PEPTIDES WITH DIRT-REMOVING ACTION FOR WASHING AND CLEANING AGENTS

Abstract

The invention relates to peptides and / or peptide conjugates as described herein. The invention further relates to washing or cleaning agents comprising at least one peptide and / or peptide conjugate as defined herein. The invention also relates to a method for cleaning textiles and / or hard surfaces using said washing or cleaning agent and the use of a peptide and / or peptide conjugate as a dirt-removing and / or dirt-repellent agent in washing and / or cleaning textiles and / or hard surfaces, as well as for improving the cleaning performance of a washing or cleaning agent containing this peptide and / or peptide conjugate.

Description

INTRODUCTION

[0001] The invention relates to peptides and / or peptide conjugates as described herein. Furthermore, the invention relates to washing or cleaning agents comprising at least one peptide and / or peptide conjugate as defined herein. Furthermore, the invention relates to a method for cleaning textiles and / or hard surfaces using said washing or cleaning agent and to the use of a peptide and / or peptide conjugate as a soil-removing and / or soil-repellent active ingredient in washing and / or cleaning textiles and / or hard surfaces, as well as to improving the cleaning performance of a washing or cleaning agent containing said peptide and / or peptide conjugate.

[0002] Intensive research is being conducted into the development of adhesive peptides. In particular, peptides that specifically bind to or interact with oxidic surfaces such as metal surfaces have already been described (WO 2014 / 072313 A1). Adhesive peptides are also of interest for many other surfaces that, due to their material or surface properties, make the treatment or attachment of other objects, substances, or compounds difficult. With such surfaces, those with low surface energies, as often found in certain plastics, are particularly problematic. Such plastics are also referred to in the art as low surface energy polymers (LSEP) and include, for example, many polyolefins or polymers with ester functions.

[0003] It is known to use “soil release polymers” in detergents for cleaning textiles to improve soil release or “soil repellent polymers” to prevent / reduce soil buildup. These soil release and / or soil repellent polymers (hereinafter referred to as SRP polymers) are water-soluble or water-dispersible polycondensates based on dicarboxylic acids and diols or cellulose ethers. SRP polymers are suspended in the wash liquor by surfactants. By diluting the wash liquor during the rinsing process, the polymer is absorbed by the textile so that the hydrophilic sides of the polymer protrude to the outside while the hydrophobic sides bind to the fiber surface. This forms a hydrophilic protective layer around the textile fiber, and dirt can only adhere to the fiber or penetrate the textile to a limited extent, making it easier to remove during the next wash cycle.SRP polymers therefore also have a positive effect on the ability of textiles to remove oil and grease. This effect is particularly evident when a textile is soiled after it has been washed several times with an SRP polymer-containing product. Accordingly, the SRP polymers only develop their full effect after several wash cycles. Typical SRP polymers can be based on copolymers of polyester and polyether, including terephthalate, such as polypropylene terephthalate. However, these polymers are typically not biodegradable.

[0004] Therefore, there is a need for alternative or improved, particularly biodegradable SRP polymers for use in detergents and cleaning agents, and / or alternatives thereto.

[0005] It has now surprisingly been found that certain peptides and / or peptide conjugates can represent a biodegradable alternative to SRP polymers. Particularly noteworthy here are peptides with a hydrophobic end and a hydrophilic end, where the hydrophobic part can bind to the textile and the hydrophilic part cannot. Particularly advantageous peptides can adhere to plastic surfaces, preferably LSEP (low surface energy polymers) surfaces, and in particular textiles made of (LSEP) plastic or with an (LSEP) plastic content. Therefore, these peptides and / or peptide conjugates are particularly suitable for use in washing and cleaning agents and can contribute to improved cleaning performance and / or impart special properties to the textiles. Furthermore, they could contribute to the degradation of synthetic and chemical substances, e.g.in detergents and cleaning products, by offering a biodegradable alternative. They could also contribute to the stabilization of other ingredients.

[0006] The invention therefore relates in a first aspect to a washing or cleaning agent, preferably a textile washing agent, comprising at least one peptide and / or peptide conjugate, wherein the at least one peptide and / or peptide conjugate has the following sequence in N- to C-terminal orientation: (Z1)p(Z2)q(Z3)r(Z4)s(Z5)t(Z6)v(Z7)w, wherein Z4 is a peptide, preferably a textile-binding peptide, selected from (A) a peptide with the following amino acid sequence: (C)mX1X2X3(X4)nX5(C)o, where C is the amino acid cysteine, where m+o = 0 or 1; where X1 is a positively charged amino acid, preferably R or K, more preferably R, X2 and X3 are uncharged amino acids, preferably A, L, S, I, M or Q, more preferably A, S, I or L, particularly preferably A or L, each X4 independently of one another is any amino acid, preferably with the exception of P, more preferably with the exception of P and G, X5 is any positively charged or uncharged amino acid, preferably R or an uncharged amino acid, more preferably Q, A or L, particularly preferably A or L, m and o are 0 or 1, where n is an integer from 0 to 46, preferably 6 to 20, more preferably 6 to 12, particularly preferably 8 to 12, (B) a peptide having an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NO: 1-27, where s = 1; where Z1 and Z7 are independently -(C2H4O) k where k = 5-100, preferably k = 20-85, preferably k = 30-75, particularly preferably k = 40-60, very particularly preferably k = 45, p and w are 0 or 1 and p+w = 0 to 2; wherein Z2 and Z6 are independently a peptide, preferably a textile-non-binding peptide, which has an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with the amino acid sequence given in SEQ ID NO:28, wherein q and v are 0 or 1 and q+v = 0 to 2; wherein Z3 and Z5 are linkers, preferably peptide linkers, wherein r and t are 0 or 1 and r+t = 0 to 2; where p+q+r+t+v+w = 0 to 6, preferably 2 to 6, more preferably 3 to 5, more preferably 3 or 4, most preferably 4.

[0007] In various designs - the peptide (A) is a peptide, where (i) the peptide has a total charge of 0 to +4, preferably 0 to +2, and / or (ii) the N-terminus comprising the first 3-4 amino acids has a positive net charge, and / or (iii) the C-terminus comprising the last 3-6 amino acids has a negative or neutral net charge and preferably comprises at least one negatively charged amino acid, in particular E, and / or (iv) the peptide does not contain P and preferably also does not contain G and even more preferably also does not contain Y; and / or - the peptide (A) is a, where (i) the sequence X1X2X3 is RSI, RAL or RLA, preferably RSI or RAL; and / or (ii) (X4) n X5 comprises at least one sequence X6X7X8, where X6 is a charged or uncharged amino acid, preferably R, K, E or Q, and X7 and X8 are independently uncharged amino acids with the exception of P and G, preferably A, L, or M, more preferably A or L, and / or (iii) the sequence (X4) nat least one aromatic amino acid, preferably W or F; and / or - the peptide (A) is a peptide, where (i) (X4) n comprises at least one sequence X6X7X8, wherein X6X7X8 is RAL or RLA, preferably RAL, and wherein this sequence is preferably located in the N-terminal amino acids of positions 4-7, and / or (ii) (X4) n X5 comprises at least one sequence X6X7X8, wherein X6X7X8 is EAL or ELA, preferably EAL, and wherein this sequence is preferably not located in the N-terminal amino acids of positions 1-6, and / or (iii) (X4) n X5 comprises at least one sequence X6X7X8, where X6X7X8 is QAL or QLA, preferably QAL; and / or - the peptide (A) consists of at least 60% and increasingly preferably at least 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75% of amino acids with a high alpha-helix-forming potential, wherein these amino acids are preferably selected from E, A, L, M, Q, K, R, F, I, H, W and D, more preferably E, A, L, M, Q, K, R, F, I and H, even more preferably E, A, L, M, Q, K, R and F; and / or - the peptide conjugate has the following structure in N- to C-terminal orientation: (i) Z1Z3Z4Z5Z7, (ii) Z2Z3Z4Z5Z6, (iii) Z1Z3Z4Z5Z6, (iv) Z2Z3Z4Z5Z7, (v) Z1Z3Z4, (vi) Z2Z3Z4, (vii) Z4Z5Z7, and (vii) Z4Z5Z6, where Z1 to Z7 are as defined above; and / or - the linker is selected from flexible linkers and rigid linkers, and / or wherein the linker is selected from the group consisting of (I) (GGGGS) n with n = 1, 2, 3, or 4; (II) (G)6; (III) (G)8; (IV) (EAAAK) nwith n = 1, 2, or 3; (V) A(EAAAK)4ALEA(EAAAK)4A; (VI) PAPAP; (VII) AEAAAKEAAAKA; and (VIII) (AP) n with n = 10-34, preferably the linker is a linker having an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences recited in SEQ ID NO:29-40.

[0008] It is particularly preferred that the at least one peptide and / or peptide conjugate is suitable for adhesion and / or binding to textiles.

[0009] It is particularly preferred that the at least one peptide and / or peptide conjugate has a dirt-repellent and / or dirt-removing effect.

[0010] It is particularly preferred that the at least one peptide and / or peptide conjugate is suitable for adhesion and / or binding to textiles, and wherein the peptide and / or peptide conjugate has a soil-repellent and / or soil-removing effect.

[0011] In preferred embodiments, the washing or cleaning agent according to the invention is a textile detergent.

[0012] The washing or cleaning agent preferably has a pH of about 6 to about 11, more preferably about 6.5 to about 10.5, even more preferably about 7 to about 10, particularly preferably about 8 to about 9.

[0013] A further aspect of the invention relates to a peptide conjugate comprising in N- to C-terminal orientation the following sequence: (Z1)p(Z2)q(Z3)r(Z4)s(Z5)t(Z6)v(Z7)w, wherein Z4 is a peptide, preferably a textile-binding peptide, selected from (A) a peptide with the following amino acid sequence: (C)mX1X2X3(X4)nX5(C)o, where C is the amino acid cysteine, where m+o = 0 or 1; where X1 is a positively charged amino acid, preferably R or K, more preferably R, X2 and X3 are uncharged amino acids, preferably A, L, S, I, M or Q, more preferably A, S, I or L, particularly preferably A or L, each X4 independently of one another is any amino acid, preferably with the exception of P, more preferably with the exception of P and G, X5 is any positively charged or uncharged amino acid, preferably R or an uncharged amino acid, more preferably Q, A or L, particularly preferably A or L, m and o are 0 or 1, where n is an integer from 0 to 46, preferably 6 to 20, more preferably 6 to 12, particularly preferably 8 to 12, (B) a peptide having an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NO: 1-27, where s = 1; where Z1 and Z7 are independently -(C2H4O) k where k = 5-100, preferably k = 20-85, preferably k = 30-75, particularly preferably k = 40-60, very particularly preferably k = 45, p and w are 0 or 1 and p+w = 0 to 2; wherein Z2 and Z6 are independently a peptide, preferably a textile-non-binding peptide, which has an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with the amino acid sequence given in SEQ ID NO:28, wherein q and v are 0 or 1 and q+v = 0 to 2; wherein Z3 and Z5 are linkers, preferably peptide linkers, wherein r and t are 0 or 1 and r+t = 0 to 2; where p+q+r+t+v+w = 2 to 6, preferably 3 to 5, particularly preferably 3 or 4, most preferably 4.

[0014] Further objects of the invention relate to - a method for cleaning textiles and / or hard surfaces, in particular dishes, characterized in that in at least one method step a washing or cleaning agent described herein is used, wherein the method is preferably carried out in a temperature range of about 20°C to about 60°C, particularly preferably about 20°C to about 40°C; and / or - the use of a washing or cleaning agent described herein for cleaning textiles and / or hard surfaces, in particular dishes, preferably in a temperature range of about 20°C to about 60°C, particularly preferably about 20°C to about 40°C; and / or - the use of a peptide according to the invention as a soil-repellent and / or soil-removing active ingredient, preferably in a temperature range of about 20°C to about 60°C, particularly preferably about 20°C to about 40°C; and / or - the use of a peptide conjugate according to the invention as a soil-repellent and / or soil-removing active ingredient, preferably in a temperature range of about 20°C to about 60°C, particularly preferably about 20°C to about 40°C; and / or - the use of a peptide according to the invention in a washing or cleaning agent to improve the cleaning performance of the washing or cleaning agent on greasy and / or oily soils, preferably in a temperature range of about 20°C to about 60°C, particularly preferably about 20°C to about 40°C; and / or - the use of a peptide conjugate according to the invention in a washing or cleaning agent to improve the cleaning performance of the washing or cleaning agent on greasy and / or oily soils, preferably in a temperature range of about 20°C to about 60°C, particularly preferably about 20°C to about 40°C.

[0015] These and other aspects, features, and advantages of the invention will become apparent to those skilled in the art from a study of the following detailed description and claims. Any feature of one aspect of the invention may be employed in any other aspect of the invention. Furthermore, it is to be understood that the examples contained herein are intended to describe and illustrate the invention, but not to limit it, and in particular, the invention is not limited to these examples. DEFINITIONS

[0016] Unless otherwise stated, all percentages are by weight (wt%), based on the total weight of the corresponding composition or agent.

[0017] Numerical ranges specified in the format "from x to y" include the specified values. If multiple preferred numerical ranges are specified in this format, it goes without saying that all ranges resulting from the combination of the different endpoints will also be included.

[0018] “At least one”, as used herein, means one or more, i.e. 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14 or more. In relation to an ingredient, the statement refers to the type of ingredient and not to the absolute number of molecules. “At least one peptide” thus means, for example, at least one type of peptide, i.e., one type of peptide or a mixture of several different peptides can be meant. Together with weight information, the statement refers to all compounds of the specified type contained in a product, i.e., the product typically does not contain any further compounds of this type beyond the stated amount of the corresponding compounds.

[0019] Unless otherwise stated, all quantities stated in connection with the washing or cleaning agents described herein refer to wt. %, based on the total weight of the composition. Furthermore, such quantities referring to at least one ingredient always refer to the total amount of that type of ingredient contained in the agent, unless explicitly stated otherwise. This means that such quantities, for example in connection with "at least one peptide," refer to the total amount of peptides contained in the agent, unless explicitly stated otherwise.

[0020] “Approximately” or “about” as used herein with reference to numerical values ​​means the corresponding value ±10%, preferably ±5%.

[0021] The term “washing and cleaning agent” or “washing or cleaning agent” as used herein is synonymous with the term “agent” and refers to a composition for cleaning textiles and / or hard surfaces, in particular dishes, as explained in the description.

[0022] "Substantially free from" as used herein means that the composition or agent contains less than 2% by weight, preferably less than 1% by weight, more preferably less than 0.5% by weight and most preferably less than 0.1% by weight of the corresponding substance, based on the total weight of the composition / agent.

[0023] "Liquid," as used herein, includes liquids and gels, as well as pasty compositions. It is preferred that the liquid compositions be flowable and pourable at room temperature, but it is also possible that they have a yield point.

[0024] A substance, e.g. a composition or an agent, is solid according to the definition of the invention if it is in the solid state at 25°C and 1,013 mbar.

[0025] A substance, e.g., a composition or agent, is liquid according to the invention's definition if it exists in the liquid state at 25°C and 1,013 mbar. Liquid also includes gel.

[0026] The term “N-terminus” or “N-terminal” in the context of the present invention typically describes the end of the amino acid chain of a peptide which has a free amino group.

[0027] The term “C-terminus” or “C-terminal” in the context of the present invention typically describes the end of the amino acid chain of a peptide which has a free carboxyl group.

[0028] The term “in N- to C-terminal orientation” in the context of this invention refers to an amino acid sequence in which the order of the amino acids is described from the N-terminus to the C-terminus.

[0029] When reference is made herein to various linked or individual amino acid sequences, these are always shown in N- to C-terminal orientation unless otherwise stated. Furthermore, the individual amino acids or amino acid sequences are linked to each other via peptide bonds unless otherwise stated. Thus, the hyphen in the peptide-linker-peptide representation, for example, means that these three corresponding sequences are fused to each other via peptide bonds.

[0030] In the context of this invention, "adhesion" or "adhesive" refers to an interaction between a peptide and / or peptide conjugate and a surface, allowing the peptide and / or peptide conjugate to adhere to the surface. Thus, the term "adhesion-promoting" refers to the ability to interact with various surfaces, e.g., textile surfaces, and / or to adhere to a specific surface under suitable conditions, i.e., usually non-denaturing conditions, with a binding affinity greater than that of a reference sequence or a reference molecule that does not exhibit adhesion-promoting properties.In this context, the term "textile-binding" refers to the ability of a molecule, in particular a peptide, to adhere to textile surfaces with a binding affinity greater than that of a reference molecule, whereas the term "textile-nonbinding" means that this ability to adhere to textile surfaces is absent. The textile-binding peptides described herein preferably exhibit 10-fold, more preferably 20-fold, 50-fold, or 100-fold higher adhesion to a given surface than any alternative peptide of comparable length that was not developed for this purpose and does not meet the sequence specifications described herein. The term "binding" in the context of this invention preferably refers to "covalent bonds" between the peptide and a surface.

[0031] The term "variant," as used herein, refers to variants of an enzyme or a protein / peptide that retain the functionality of the parent molecule, but differ from the parent sequence by one or more sequence variations, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, or more sequence variations, e.g., a substitution, deletion, or insertion. The sequence identity of such variants may be in the range of 80% relative to the total length of the parent peptide, and may be at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 99.5%. DETAILED DESCRIPTION

[0032] The present invention is based on the surprising discovery of the inventors that certain peptides and / or peptide conjugates, when used in detergents or cleaning agents, not only provide improved cleaning performance on greasy and / or oily soils, but also exhibit a dirt-removing and / or dirt-repellent effect. They thus represent a biodegradable alternative to SRP polymers. Particularly noteworthy here are peptides with a hydrophobic end and a hydrophilic end, in which the hydrophobic part can bind to the textile and the hydrophilic part cannot. Particularly advantageous peptides can adhere to plastic surfaces, preferably LSEP (low surface energy polymers) surfaces, and in particular textiles made of (LSEP) plastic or containing (LSEP) plastic.Therefore, these peptides and / or peptide conjugates are particularly suitable for use in detergents and cleaning agents, and can contribute to improved cleaning performance and / or impart special properties to textiles. Furthermore, they could help reduce or completely eliminate synthetic and chemical substances, e.g., in detergents and cleaning agents, by providing a biodegradable alternative. They could also contribute to the stabilization of other ingredients.

[0033] This is particularly surprising insofar as such peptides and / or peptide conjugates have so far been associated neither with a soil-removing and / or soil-repellent effect nor with an improved cleaning performance of washing or cleaning agents, in particular not with regard to greasy and / or oily soils. Textile-binding peptides

[0034] According to the invention, the washing or cleaning agent comprises at least one peptide selected from (A) a peptide comprising or consisting of an amino acid sequence of 4 to 50 amino acids, preferably 10 to 24 amino acids, more preferably 10 to 16 amino acids, particularly preferably 12 to 16 amino acids, wherein the amino acid sequence in N- to C-terminal orientation has the following sequence: (C)mX1X2X3(X4)nX5(C)o, where X1 is a positively charged amino acid, preferably R or K, more preferably R, X2 and X3 are uncharged amino acids, preferably A, L, S, I, M or Q, more preferably A, S, I or L, particularly preferably A or L, each X4 independently of one another is any amino acid, preferably with the exception of P, more preferably with the exception of P and G, X5 is any positively charged or uncharged amino acid, preferably R or an uncharged amino acid, more preferably Q, A or L, particularly preferably A or L, m and o are 0 or 1, where m+o = 0 or 1, and n is an integer from 0 to 46, preferably 6 to 20, more preferably 6 to 12, particularly preferably 8 to 12; and / or (B) a peptide having an amino acid sequence which has at least 80%, and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with any of the amino acid sequences set out in SEQ ID NO:1-27.

[0035] The peptide comprises or consists of an amino acid sequence of 4 to 50 amino acids in length, preferably of at least 8, 9, 10, 11, or 12 amino acids in length. Preferred lengths are up to 40, up to 35, up to 30, or up to 25, or up to 24 amino acids. For example, the peptide can have a length of 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, or 24 amino acids, in particular 12 to 18 amino acids. The peptide is preferably a peptide comprising or consisting of an amino acid sequence with 4 to 50 amino acids, preferably 10 to 24 amino acids, more preferably 10 to 16 amino acids, particularly preferably 12 to 16 amino acids, e.g. 12, 13, 14, 15, or 16 amino acids.

[0036] In a preferred embodiment, the peptide has the following amino acid sequence in N- to C-terminal orientation: (C)mX1X2X3(X4)nX5(C)o, where X1 is a positively charged amino acid, preferably R or K, more preferably R, X2 and X3 are uncharged amino acids, preferably A, L, M, S, I or Q, more preferably A, S, I or L, particularly preferably A or L, each X4 independently of one another is any amino acid, preferably with the exception of P, more preferably with the exception of P and G, X5 is any positively charged or uncharged amino acid, preferably R or an uncharged amino acid, more preferably Q, A or L, particularly preferably A or L, m and o are 0 or 1, where m+o = 0 or 1, and n is an integer from 0 to 46, preferably from 6 to 20, e.g. 9, 10, 11, 12 or 13.

[0037] Alternatively or additionally, the peptide comprises or consists of an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NO:1-27.

[0038] A "peptide" in the context of the present invention is understood to mean a polymer composed of amino acids, preferably the 20 proteinogenic L-amino acids, preferably of a linear structure, which has up to 100 amino acids linked to one another via peptide bonds. According to the invention, the peptides of the invention have an amino acid sequence of 4 to 50 amino acids. The amino acids are specified in the context of this invention in a one-letter code, where, for example, C stands for cysteine, R for arginine, A for alanine, and L for leucine. In particular, "C" in the above sequence (C) m X1X2X3(X4)n X5(C) o for a cysteine ​​residue. It is further understood that, unless otherwise stated, the amino acids in an amino acid sequence disclosed herein are linked via peptide bonds and, unless otherwise stated, the sequence is listed in N- to C-terminal orientation.

[0039] Peptides can be chemically synthesized in various ways and / or produced recombinantly by protein design. Short peptides are now easily synthesized, e.g., via solid-phase synthesis. Longer peptides and polypeptides, on the other hand, are often also produced recombinantly in the host organism.

[0040] Typical acidic or negatively charged amino acids (depending on the pH value) are D and E.

[0041] Positively charged or basic amino acids (depending on pH) typically include R, K, and H.

[0042] Amino acids such as G, A, C, I, L, M, F, V, P, S, T, W, Y, N and Q are typically uncharged, i.e. neutral amino acids.

[0043] When reference is made herein to an "any" amino acid, this typically means one of the 20 naturally occurring proteinogenic amino acids, i.e., one of glycine (G), alanine (A), valine (V), leucine (L), isoleucine (I), phenylalanine (F), serine (S), threonine (T), proline (P), methionine (M), cysteine ​​(C), histidine (H), lysine (K), arginine (R), glutamine (Q), asparagine (N), aspartic acid (D), glutamic acid (E), tyrosine (Y), and tryptophan (W). The amino acids are typically L-amino acids unless otherwise stated. In alternative embodiments, the peptide may also consist of D-amino acids, although it may be preferred that D- and L-amino acids do not occur simultaneously within the peptides described herein. In various embodiments, such an arbitrary amino acid encompasses all of the aforementioned amino acids with the exception of proline, or in some embodiments also with the exception of proline and glycine.These two amino acids are not preferred in certain embodiments because they exhibit helix-breaking properties and can therefore adversely affect the secondary structure of the peptides.

[0044] In preferred embodiments, the peptide has a total charge of -2 to +12, preferably from 0 to +8, more preferably 0 to +4, particularly preferably 0 to +2. The total charge of the peptide is based on the number of positively and negatively charged amino acids in the peptide, in particular arginine (R), lysine (K), histidine (H), aspartic acid (D), and glutamic acid (E), and results from the sum of the negative and positive charges, with one positive and one negative charge canceling each other out. A peptide with 2 arginine residues and 1 glutamic acid residue would therefore have a total charge of +1. The total charge of the peptide is preferably -2 to +12, more preferably 0 to +8, more preferably 0 to +4, most preferably 0 to +2.

[0045] In preferred embodiments, the peptide according to the invention comprises: (i) a total charge of -2 to +12, preferably 0 to +8, more preferably 0 to +4, most preferably 0 to +2; and / or (ii) a positive net charge at the N-terminus, which comprises the first 3-4 amino acids; and / or (iii) at the C-terminus, which comprises the last 3-6 amino acids, a negative or neutral net charge, preferably at least one negatively charged amino acid, in particular E; and / or (iv) no P and more preferably no G and in particular no Y.

[0046] All of the above features, in particular (i)-(iv), may be implemented individually or in any combination.

[0047] The feature that the peptide has a positive net charge at the "N-terminus, which comprises the first 3-4 amino acids," means that the N-terminal 3-4 amino acids comprise more positively charged than negatively charged amino acids. In various embodiments, this feature is met, for example, when the N-terminal 3-4 amino acids contain 1 or 2 positively charged amino acids, i.e., H, K, or R, preferably K or R, more preferably R, and no negatively charged amino acids such as E or D. If the N-terminus contains a negatively charged amino acid, the number of positively charged amino acids must be at least 2 for the net charge to remain positive.

[0048] The characteristic that the peptide has a negative or neutral net charge at the C-terminus, which encompasses the last 3-6 amino acids, means that the number of charged amino acids must be 0, or the number of negatively charged amino acids, i.e., D and E, must be greater than the number of positively charged ones. An example of such a C-terminal sequence would be EAL or the double sequence of this motif.

[0049] In various preferred embodiments, the sequence X1X2X3 is RAL, RSI, or RLA, preferably RAL or RLA, especially RAL. The N-terminal sequence RAL or RLA not only advantageously has a positive net charge, it also comprises amino acids with a particularly high alpha-helix-forming potential, as explained further below. In some embodiments, the arginine residue can also be replaced by lysine, but the N-terminal arginine residue is particularly preferred.

[0050] Furthermore, it is preferred that (i) the sequence (X4) n X5 comprises at least one sequence X6X7X8, where X6 is a charged or uncharged amino acid, preferably R, K, E, L, A or Q, more preferably R, K, E or Q, and X7 and X8 are independently negatively charged or uncharged amino acids with the exception of P and G, preferably A, L, E, R, Q or M, e.g. A, L, E, Q or M, more preferably A, E, Q or L, even more preferably A, E or L, particularly preferably A or L; and / or (ii) (X4) n at least one aromatic amino acid, preferably W or F.

[0051] If the sequence X6X7X8 includes an X6 which is R or K, the sequence X6X7X8 is preferably not at the C-terminus and preferably not within the 6 C-terminal amino acids. In such cases, the sequence (X4) nX5 comprise one or more further sequences X6X7X8 which are located C-terminal to the sequence which comprises a positively charged amino acid as X6, wherein these further sequences then preferably do not have a positively charged amino acid as X6.

[0052] It is preferred that one of the sequences X6X7X8, which are close, ie within the 6 C-terminal amino acids, or at the C-terminus, has as X6 a negatively charged amino acid, e.g. E.

[0053] If, in some embodiments, the peptide contains an aromatic amino acid selected from W and F, there is a positively or negatively charged amino acid next to, in particular C-terminally, and in particular there is no further aromatic amino acid next to the aromatic amino acid.

[0054] The aromatic amino acids phenylalanine (F) and tryptophan (W) are preferably used in the peptide sequence according to the invention as helix formers and / or for pi stacking. The aromatic amino acid tyrosine (Y) is not used in various embodiments of the peptide sequence because of its helix-breaking properties. Therefore, in various embodiments, the peptide is free of Y residues.

[0055] In the context of the present invention, “pi-stacking” refers to the non-covalent interaction between aromatic ring systems.

[0056] Preferably includes (i) (X4) n at least one sequence X6X7X8, where X6X7X8 is RAL or RLA, preferably RAL, and where this sequence is preferably located in the N-terminal amino acids of positions 4-7 or at least 6-7 amino acids from the C-terminus; and / or (ii) (X4) nX5 comprises at least one sequence X6X7X8, wherein X6X7X8 is EAL, LEA or ELA, preferably EAL, and wherein this sequence is preferably not located in the N-terminal amino acids of positions 1-6; and / or (iii) (X4) n X5 comprises at least one sequence X6X7X8, where X6X7X8 is EQA, QAL, LQA or QLA, preferably EQA, QAL or QLA, in particular QAL.

[0057] In other possible embodiments, (X4) comprises n X5 at least one sequence X6X7X8, where X6X7X8 is QLA or EQA, said sequence preferably not being located in the N-terminal amino acids of positions 1-6 or 1-11.

[0058] It is also possible that (X4) n X5 comprises at least one sequence X6X7X8X9, where X6X7X8X9 is AQLA or SEQA, said sequence preferably not being located in the N-terminal amino acids of positions 1-6 or 1-11.

[0059] In preferred embodiments, the peptide comprises the sequence X1X2X3, where X1X2X3 is RAL, and (X4) n X5 comprises at least one of QAL and EAL, preferably both. In such embodiments, the peptide has the sequence (C) m RAL(X 10 )qQAL(X 11 ) r EAL(X 12 ) s (C) o or (C) m RAL(X 10 ) q EAL(X 11 ) r QAL(X 12 ) s (C) o , where X 10 and X 11 are independently any amino acid, preferably with the exception of P, more preferably with the exception of P and G, X 12is any uncharged amino acid, preferably Q, A or L, more preferably A or L, q and r are 0 or integers from 1-10, preferably 0, 1, 2 or 3 and s is 0 or 1, where q+r+s = 0-21, preferably 0-15 or 0-9 or 1-15 or 1-9 or 1-6 or 0-6 or 0-3 or 1-3.

[0060] Furthermore, it is preferred that the peptide additionally comprises at least one further (second) RAL sequence. In various embodiments, this can be located directly C-terminally after the first RAL sequence or separated from it by 1-3 amino acids, e.g., by 1, 2, or 3 amino acids.

[0061] In preferred embodiments, the peptide contains two RAL sequences and at least one EAL and one QAL sequence. Preferred sequences are: • RALRAL(X 10 ) q QAL(X 11 ) r EAL(X 12 ) s , • RALRAL(X 10 ) q EAL(X 11 ) r QAL(X 12) s , • RAL(X 10 ) q RALQAL(X 11 ) r EAL(X 12 ) s , • RAL(X 10 ) q RALEAL(X 11 ) r QAL(X 12 ) s , • RAL(X 10 ) q QALRAL(X 11 ) r EAL(X 12 ) s , • RAL(X 10 ) q EALRAL(X 11 ) r QAL(X 12 ) s ,where X 10 and X 11 independently of one another are any amino acid, preferably with the exception of P, more preferably with the exception of P and G, e.g. W or F or further motifs QAL or EAL, X 12 is any uncharged amino acid, preferably Q, A or L, more preferably A or L, q and r are 0 or integers from 1-6, preferably 0, 1, 2, or 3, and s is 0 or 1, preferably 0, where q+r = 0-9, preferably 0-6 or 0-3 or 1-9 or 1-6 or 1-3.

[0062] Furthermore, in various embodiments, it is preferred that the peptide contains at least one W or F, preferably exactly one W or F.

[0063] Preferably, the peptide comprises amino acids with a high alpha-helix-forming potential, wherein these amino acids are selected from E, A, L, M, Q, K, R, F, I, H, W and D, more preferably from E, A, L, M, Q, K, R, F, I and H; most preferably from E, A, L, M, Q, K, R and F.

[0064] In preferred embodiments, the peptide consists of at least 60% and increasingly preferably at least 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94% or 95% amino acids with a high alpha-helix-forming potential, wherein these amino acids are preferably selected from E, A, L, M, Q, K, R, F, I, H, W and D, more preferably from E, A, L, M, Q, K, R, F, I and H; particularly preferably from E, A, L, M, Q, K, R and F.

[0065] The peptide according to the invention particularly preferably forms a helical secondary structure, in particular an alpha-helix structure, preferably with an alpha-helix content of at least 80% and increasingly preferably of at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, or 95%, in particular higher than 95%. The use of the motif AL or LA in the amino acid sequence of the peptide according to the invention can contribute to the stability of the helix structure because these amino acids have a high alpha-helix-forming potential.

[0066] In preferred embodiments, the peptide has an amino acid sequence according to one of SEQ ID NO:1-15, or variants thereof, which have at least 80%, and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, and less than 100% sequence identity to the specified sequence, wherein preferably the RAL motif, and more preferably also the EAL and / or QAL motif, if present, are invariable. If the RAL, EAL, and QAL motifs are present in the peptide, they are preferably invariable in all of the aforementioned variants.

[0067] In various embodiments, the peptide may have a high proportion of hydrophobic amino acids selected from A, L, F, W, V, M, I and P, in particular A, L, F, W, V, M and I.

[0068] Preferably, the peptide has an amino acid sequence which has a length of 10 to 24 amino acids, e.g. 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23 or 24 amino acids, in particular 12 to 19 amino acids, e.g. 12 to 18 amino acids.

[0069] In some embodiments, the peptide has the amino acid cysteine ​​(C) at the C-terminus. In other embodiments, the peptide has the amino acid cysteine ​​at the N-terminus. This amino acid can enable coupling to other molecules, structures, or substrates via the free sulfhydryl group. This amino acid therefore serves as a linkage site but is typically not involved in the desired adhesive effect. The peptide can also have no C at either the N-terminus or the C-terminus.

[0070] Preferably, the peptide comprises or consists of an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one of the following amino acid sequences: • RALQALRALQALEAL (SEQ ID NO:1), • RALRALRALEALEAL (SEQ ID NO:2), • RALRALRALQALQAL (SEQ ID NO:3), • RALRALRALQALEAL (SEQ ID NO:4), • RALRALQALEEALEAL (SEQ ID NO:5), • RALFEALQALFRALEAL (SEQ ID NO:6), • RALRALEALQALEA (SEQ ID NO:7), • RALFEALFRALEALR (SEQ ID NO:8), • RALFEALFRALEAL (SEQ ID NO:9), • RALEALFRALEAL (SEQ ID NO:10), • RALRALFEALEAL (SEQ ID NO:11), • RALEALFRALQALEAL (SEQ ID NO:12), • RALEALWRALQALEAL (SEQ ID NO:13), • RALEALWRALEAL (SEQ ID NO:14), • RALARALARALAQALA (SEQ ID NO:15), • RSIVTFSLRQNAQLA (SEQ ID NO:16), • RSIVTFSLRQNSEQA (SEQ ID NO:17), • GLHTSATNLYLH (SEQ ID NO:18), • QHSIRLLTIKKP (SEQ ID NO:19), • QQSIRIMTIKHP (SEQ ID NO:20), • WRHPRLRCGNLL (SEQ ID NO:21), • QKSRNRMTRTHP (SEQ ID NO:22), • SRARLFVVTYHK (SEQ ID NO:23), • HMISTMNAASRR (SEQ ID NO:24), • RSIVTFSLRQNR (SEQ ID NO:25), • RNTIRIRTIKHP (SEQ ID NO:26), • RHSSTLRYRPLP (SEQ ID NO:27).

[0071] Variants of the peptides according to the invention, the amino acid sequence of which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one of the amino acid sequences which correspond to the sequences in SEQ ID NO:1-27, preferably differ in a maximum of 3 positions, more preferably in a maximum of 2 positions, particularly preferably in a maximum of 1 position from one of the amino acid sequences which correspond to the sequences in SEQ ID NO:1-27. For example, if one position is different, either one of the amino acids in the respective sequence may have been swapped, or the sequences may be identical, but an amino acid has been added or omitted within the amino acid chain or at the N- or C-terminal positions. For example, a cysteine ​​(C) may have been added at the C- or N-terminal positions.

[0072] The peptide according to the invention particularly preferably has a sequence which is shown in SEQ ID NO:1-27.

[0073] Particularly preferably, the peptide has a sequence according to SEQ ID NO:25 or SEQ ID NO:1 or SEQ ID NO:5, or is a variant thereof, wherein a variant has an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with one of the amino acid sequences.

[0074] Particularly preferred peptides according to the invention are textile-binding peptides, ie peptides which have the ability to adhere to textile surfaces under suitable conditions, ie usually non-denaturing conditions, and thus have adhesive properties.

[0075] Good adhesion to textile surfaces, in particular textile surfaces made of synthetic fibers, such as polyester-containing textiles, can be achieved, for example, by a peptide with a pronounced helix structure (in particular alpha-helix structure) and / or a high arginine content, in particular at one of the termini.

[0076] Preferred peptides which have good adhesion, in particular to plastic, preferably polyester, have an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one of the amino acid sequences given in SEQ ID NO: 1-27. Particularly preferred peptides which have good adhesion, in particular to plastic, preferably polyester. Plastic, preferably polyester, have good adhesion, have an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one of the amino acid sequences given in SEQ ID NO: 1, 5 or 25. Very particularly preferred peptides which are particularly resistant toPlastic, preferably polyester, have good adhesion, have an amino acid sequence that is identical to one of the amino acid sequences given in SEQ ID NO:1-27.

[0077] Preferred peptides which are textile-binding within the meaning of the invention and have good adhesion to plastic-containing textiles, preferably polyester-containing textiles, have an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one of the amino acid sequences given in SEQ ID NO: 1-27. Particularly preferred peptides which are textile-binding within the meaning of the invention and have good adhesion to plastic-containing textiles, preferably polyester-containing textiles. plastic-containing, preferably polyester-containing, textiles have good adhesion, have an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one of the amino acid sequences given in SEQ ID NO: 1, 5 or 25.Very particularly preferred peptides which are textile-binding within the meaning of the invention and have good adhesion to plastic-containing, preferably polyester-containing textiles, have an amino acid sequence which is identical to one of the amino acid sequences given in SEQ ID NO:1-27.

[0078] Preferred peptides which are textile-binding within the meaning of the invention and have good adhesion to plastic-containing mixed fabrics, preferably polyester-containing mixed fabrics, in particular polyester / cotton mixed fabrics, have an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one of the amino acid sequences given in SEQ ID NO: 1-27. Particularly preferred peptides which are textile-binding within the meaning of the invention and have good adhesion to plastic-containing mixed fabrics, preferably polyester-containing mixed fabrics, in particular polyester / cotton mixed fabrics.plastic-containing mixed fabrics, preferably polyester-containing mixed fabrics, in particular polyester / cotton mixed fabrics, have good adhesion, have an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity to one of the amino acid sequences given in SEQ ID NO: 1, 5 or 25. Very particularly preferred peptides which are textile-binding within the meaning of the invention and compared to plastic-containing mixed fabrics, preferably polyester-containing mixed fabrics, in particular polyester / cotton mixed fabrics, have good adhesion, have an amino acid sequence which is identical to one of the amino acid sequences given in SEQ ID NO:1-27.

[0079] Methods for determining adhesion are known to the person skilled in the art and any suitable methods can be used.

[0080] A common method for determining adhesion is based on a direct measurement method using µBCA. For this purpose, cloth patches are mixed with a peptide solution to be tested (0.02 mg / ml in distilled water), incubated for 1 h at room temperature with shaking (750 rpm), and washed (3x with 0.5 ml distilled water, shaking at 750 rpm for 5 min). Subsequently, 0.2 ml distilled water and 0.2 ml BCA reagent are added and incubated for 60 min at 60°C. The absorbance is then measured at 562 nm. An adhesion point after an infinite adhesion time can be determined from the measured adhesion values. AP in % shows what percentage of the applied amount (100%) remains on the cloth patch after washing. The higher the AP value, the higher the binding affinity and thus the adhesion. (<20% = no adhesion; 21 to 40% = poor adhesion; 41 to 60% = moderate adhesion; 61 to 80% = good adhesion; >80% = very good adhesion).

[0081] Another detection method for determining adhesion is based on the fluorescence method described here in the examples.

[0082] Other methods for determining adhesion known to the person skilled in the art can also be used.

[0083] A peptide is a textile-binding peptide within the meaning of the invention if the ability of the peptide to adhere to textile surfaces is demonstrated in one of the methods mentioned, wherein the binding affinity is greater than that of a reference molecule and wherein the textile-binding peptides described herein preferably have 10-fold, more preferably 20-fold, 50-fold or 100-fold higher adhesion to a given surface than any alternative peptide of comparable length which was not developed for this purpose and does not meet the sequence specifications described herein.

[0084] A peptide is, in the sense of the invention, a textile-binding peptide in particular if the ability of the peptide to adhere to textile surfaces is demonstrated in a method according to Example 2, wherein the binding affinity is greater than that of a reference molecule.

[0085] A peptide is, in the sense of the invention, in particular a textile-binding peptide if the ability of the peptide to adhere to textile surfaces is demonstrated in a previously described BCA method, wherein the AP value is greater than 61% and preferably greater than 80%. Textile non-binding peptide

[0086] Alternatively or additionally, the washing or cleaning agent according to the invention comprises at least one peptide conjugate, which may contain a textile-nonbinding peptide. In this context, "textile-nonbinding" means that textile-nonbinding peptides do not have the ability to adhere to textile surfaces.

[0087] According to the invention, the textile-non-binding peptide is a peptide which has an amino acid sequence according to SEQ ID NO:28, or is a variant thereof, wherein the variant has an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% sequence identity with the amino acid sequence in SEQ ID NO:28.

[0088] Most preferably, the textile-nonbinding peptide has the following amino acid sequence: • NGLLIPQFLVAS (SEQ ID NO:28).

[0089] A peptide is a textile-non-binding peptide within the meaning of the invention if the ability of the peptide to adhere to textile surfaces is not demonstrated in one of the methods mentioned, whereby the binding affinity is lower than or equal to that of a reference molecule.

[0090] A peptide is, in the sense of the invention, a textile-non-binding peptide in particular if, in a method according to Example 2, the ability of the peptide to adhere to textile surfaces is not demonstrated, wherein the binding affinity is lower than or equal to that of a reference molecule.

[0091] A peptide is, in the sense of the invention, a textile-non-binding peptide in particular if the ability of the peptide to adhere to textile surfaces is not demonstrated in a previously described BCA method, wherein the AP value is less than 20%. Peptide conjugate

[0092] Alternatively or additionally, the washing or cleaning agent according to the invention comprises at least one peptide conjugate comprising in N- to C-terminal orientation the following sequence (Z1)p(Z2)q(Z3)r(Z4)s(Z5)t(Z6)v(Z7)w, wherein Z4 is a peptide, preferably a textile-binding peptide, selected from (A) a peptide with the following amino acid sequence: (C)mX1X2X3(X4)nX5(C)o, where C is the amino acid cysteine, where m+o = 0 or 1; where X1 is a positively charged amino acid, preferably R or K, more preferably R, X2 and X3 are uncharged amino acids, preferably A, L, S, I, M or Q, more preferably A, S, I or L, particularly preferably A or L, each X4 independently of one another is any amino acid, preferably with the exception of P, more preferably with the exception of P and G, X5 is any positively charged or uncharged amino acid, preferably R or an uncharged amino acid, more preferably Q, A or L, particularly preferably A or L, m and o are 0 or 1, where n is an integer from 0 to 46, preferably 6 to 20, more preferably 6 to 12, particularly preferably 8 to 12, (B) a peptide having an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NO:1-27, where s = 1; where Z1 and Z7 are independently -(C2H4O) k where k = 5-100, preferably k = 20-85, preferably k = 30-75, particularly preferably k = 40-60, very particularly preferably k = 45, p and w are 0 or 1 and p+w = 0 to 2; wherein Z2 and Z6 are independently a peptide, preferably a textile-non-binding peptide, which has an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with the amino acid sequence given in SEQ ID NO:28, wherein q and v are 0 or 1 and q+v = 0 to 2; wherein Z3 and Z5 are linkers, preferably peptide linkers, wherein r and t are 0 or 1 and r+t = 0 to 2; where p+q+r+t+v+w = 2 to 6, preferably 3 to 5, particularly preferably 3 or 4, most preferably 4.

[0093] According to the invention, the peptides contained in the peptide conjugate according to the invention are as defined hereinbefore, namely textile-binding peptides and / or textile-non-binding peptides.

[0094] According to the invention, the textile-binding peptide contained in a peptide conjugate according to the invention is as defined above in the section "Textile-binding peptide." According to the invention, the textile-nonbinding peptide contained in a peptide conjugate according to the invention is as defined above in the section "Textile-nonbinding peptide."

[0095] In preferred embodiments, the peptide conjugate contains at least one textile-binding peptide, as defined herein, and at least one textile-nonbinding peptide, as defined herein. In further preferred embodiments, the peptide conjugate contains at least one textile-binding peptide, as defined herein, and at least two textile-nonbinding peptides, as defined herein. Particularly preferably, the peptide conjugate contains one textile-binding peptide and two textile-nonbinding peptides.

[0096] In various embodiments, when more than one textile-binding peptide is present in the peptide conjugate, these may be the same or different. In preferred embodiments, they are the same.

[0097] In various embodiments, when more than one textile-nonbinding peptide is present in the peptide conjugate, these may be the same or different. In preferred embodiments, they are the same.

[0098] In various embodiments, the peptide conjugate is N- and / or C-terminally modified, in particular pegylated. In preferred embodiments, the peptide conjugate is N-terminally modified, in particular pegylated. In preferred embodiments, the peptide conjugate is C-terminally modified, in particular pegylated. In particularly preferred embodiments, the peptide conjugate is N- and C-terminally modified, in particular pegylated.

[0099] The term “pegylated” or “pegylation” in the context of the present invention means that a -(C2H4O) k-group, where k = 5-100, preferably k = 20-85, more preferably k = 30-75, more preferably k = 40-60, most preferably k = 45, is linked to the terminal amino acid at the N- and / or C-terminus of a peptide. PEGylation is a process in which polyethylene glycol (PEG) chains are attached to proteins, which can improve their stability, solubility, and therapeutic properties. While many PEGylation processes involve the use of reactive cysteine ​​residues on proteins, it is indeed possible to PEGylate proteins without cysteine ​​residues. Other amino acids that can form a covalent bond with PEG or PEG derivatives include lysine (ε-amino group), histidine (imidazole side chain), or aspartic acid / glutamic acid (carboxyl groups). PEGylation can be achieved by various chemical reactions, whereby peptide PEGylation functions analogously to protein PEGylation (see, for example, Santos et al., Protein PEGylation for the design of biobetters: from reaction to purification processes, Braz. J. Pharm. Sci. 2018, 54(Special):e01009). This disclosure is expressly incorporated by reference, and the disclosure content therein is incorporated into the present patent application. One common method is the use of reactive polyethylene glycol (PEG) derivatives. These derivatives have functional groups such as NHS esters or maleimide, which can react with functional groups of the peptide molecule. The peptide and PEG derivatives are mixed together under suitable conditions (pH, temperature) to start the coupling reaction. N-terminal PEGylation is achieved, for example, using polyethylene glycol N-hydroxysuccinimide (PEG-NHS). C-terminal PEGylation is achieved, for example, by Michael addition of polyethylene glycol maleimide to the thiol group of a terminal cysteine.Alternatively, C-terminal PEGylation can also be achieved by adding polyethylene glycol maleimide to the OH group of any terminal amino acid.

[0100] In preferred embodiments, the PEG group at the C- and / or N-terminus comprises about 5 to about 100 ethylene glycol units, preferably about 20 to about 85 ethylene glycol units, more preferably about 30 to about 75 ethylene glycol units, more preferably about 40 to about 60 ethylene glycol units, most preferably about 45 ethylene glycol units. In preferred embodiments, the PEG group at the C- and / or N-terminus has a molecular weight of about 220 g / mol to about 4400 g / mol, preferably about 880 g / mol to about 3740 g / mol, more preferably about 1320 g / mol to about 3300 g / mol, more preferably about 1760 g / mol to about 2640 g / mol, most preferably about 2000 g / mol.

[0101] In preferred embodiments, the PEG group at the C-terminus comprises about 5 to about 100 ethylene glycol units, preferably about 20 to about 85 ethylene glycol units, more preferably about 30 to about 75 ethylene glycol units, more preferably about 40 to about 60 ethylene glycol units, most preferably about 45 ethylene glycol units. In preferred embodiments, the PEG group at the C-terminus has a molecular weight of about 220 g / mol to about 4400 g / mol, preferably about 880 g / mol to about 3740 g / mol, more preferably about 1320 g / mol to about 3300 g / mol, more preferably about 1760 g / mol to about 2640 g / mol, most preferably about 2000 g / mol.

[0102] In preferred embodiments, the PEG group at the N-terminus comprises about 5 to about 100 ethylene glycol units, preferably about 20 to about 85 ethylene glycol units, preferably about 30 to about 75 ethylene glycol units, more preferably about 40 to about 60 ethylene glycol units, most preferably about 45 ethylene glycol units. In preferred embodiments, the PEG group at the N-terminus has a molecular weight of about 220 g / mol to about 4400 g / mol, preferably about 880 g / mol to about 3740 g / mol, preferably about 1320 g / mol to about 3300 g / mol, more preferably about 1760 g / mol to about 2640 g / mol, most preferably about 2000 g / mol.

[0103] In preferred embodiments, the PEG group at the C- and N-terminus comprises about 5 to about 100 ethylene glycol units, preferably about 20 to about 85 ethylene glycol units, preferably about 30 to about 75 ethylene glycol units, more preferably about 40 to about 60 ethylene glycol units, most preferably about 45 ethylene glycol units. In preferred embodiments, the PEG group at the C- and N-terminus has a molecular weight of about 220 g / mol to about 4400 g / mol, preferably about 880 g / mol to about 3740 g / mol, preferably about 1320 g / mol to about 3300 g / mol, more preferably about 1760 g / mol to about 2640 g / mol, most preferably about 2000 g / mol.

[0104] In various embodiments of the invention, the PEG group and / or the at least one, preferably at least two, textile-non-binding peptide(s) are directly covalently linked to the at least one textile-binding peptide, i.e. the first and / or last amino acid of the respective peptides are linked to one another via a peptide bond. Alternatively, the bond can also be formed via a linker, in particular a peptide linker. Such a bond via a peptide linker is preferred. Suitable linkers are known in the art and can be static / rigid or flexible. This property is determined by the secondary structure of the linker; for example, rigid linkers can have an alpha helix as their secondary structure. In various embodiments, the peptide linker sequence is flexible and has no secondary structure or only short secondary structure elements. Linkers suitable in the context of the present invention are described below.

[0105] Linkers suitable in the context of the present invention, which are preferably peptide linkers, can be divided into flexible linkers and rigid linkers. Such linkers are generally known in the prior art (Chen et al. (2013) Fusion protein linkers: Property, design and functionality, Advanced Drug Delivery Reviews, 65 (10): 1357-1369).

[0106] If the peptide conjugate according to the invention comprises at least one linker, the linker represents the covalent bond of the peptides to be linked or the peptides with the PEG group, and the corresponding peptide conjugate has the following structure in N- to C-terminal orientation: (i) Z1Z3Z4Z5Z7, (ii) Z2Z3Z4Z5Z6, (iii) Z1Z3Z4Z5Z6, (iv) Z2Z3Z4Z5Z7, (V) Z1Z3Z4, (vi) Z2Z3Z4, (vii) Z4Z5Z7, or (viii) Z4Z5Z6,wherein Z4 is a peptide, preferably a textile binding peptide, selected from (A) a peptide with the following amino acid sequence: (C)mX1X2X3(X4)nX5(C)o, where C is the amino acid cysteine, where m+o = 0 or 1; where X1 is a positively charged amino acid, preferably R or K, more preferably R, X2 and X3 are uncharged amino acids, preferably A, L, S, I, M or Q, more preferably A, S, I or L, particularly preferably A or L, each X4 independently of one another is any amino acid, preferably with the exception of P, more preferably with the exception of P and G, X5 is any positively charged or uncharged amino acid, preferably R or an uncharged amino acid, more preferably Q, A or L, particularly preferably A or L, m and o are 0 or 1, where n is an integer from 0 to 46, preferably 6 to 20, more preferably 6 to 12, particularly preferably 8 to 12, (B) a peptide having an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NO:1-27, where s = 1; where Z1 and Z7 are independently -(C2H4O) k where k = 5-100, preferably k = 20-85, preferably k = 30-75, particularly preferably k = 40-60, p and w are 0 or 1 and p+w = 0 to 2; wherein Z2 and Z6 are independently a peptide, preferably a textile-non-binding peptide, which has an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with the amino acid sequence given in SEQ ID NO:28, wherein q and v are 0 or 1 and q+v = 0 to 2; wherein Z3 and Z5 are linkers, preferably peptide linkers, wherein r and t are 0 or 1 and r+t = 0 to 2; where p+q+r+t+v+w = 2 to 6, preferably 3 to 5, particularly preferably 3 or 4, most preferably 4.

[0107] In preferred embodiments, the peptide conjugate has the following structure in N- to C-terminal orientation: (i) Z1Z3Z4Z5Z7, (ii) Z2Z3Z4Z5Z6, (iii) Z1Z3Z4Z5Z6, (iv) Z2Z3Z4Z5Z7, (v) Z1Z3Z4, (vi) Z2Z3Z4, (vii) Z4Z5Z7, or (viii) Z4Z5Z6,wherein Z4 is a peptide, preferably a textile binding peptide, selected from (A) a peptide with the following amino acid sequence: (C)mX1X2X3(X4)nX5(C)o, where C is the amino acid cysteine, where m+o = 0 or 1; where X1 is a positively charged amino acid, preferably R or K, more preferably R, X2 and X3 are uncharged amino acids, preferably A, L, S, I, M or Q, more preferably A, S, I or L, particularly preferably A or L, each X4 independently of one another is any amino acid, preferably with the exception of P, more preferably with the exception of P and G, X5 is any positively charged or uncharged amino acid, preferably R or an uncharged amino acid, more preferably Q, A or L, particularly preferably A or L, m and o are 0 or 1, where n is an integer from 0 to 46, preferably 6 to 20, more preferably 6 to 12, particularly preferably 8 to 12, (B) a peptide having an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NO:1-27, where s = 1; where Z1 and Z7 are independently -(C2H4O) k where k = 5-100, preferably k = 20-85, preferably k = 30-75, particularly preferably k = 40-60, p and w are 0 or 1 and p+w = 0 to 2; wherein Z2 and Z6 are independently a peptide, preferably a textile-non-binding peptide, which has an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with the amino acid sequence given in SEQ ID NO:28, wherein q and v are 0 or 1 and q+v = 0 to 2; wherein Z3 and Z5 are linkers, preferably peptide linkers, wherein r and t are 0 or 1 and r+t = 0 to 2; where p+q+r+t+v+w = 2 to 6, preferably 3 to 5, particularly preferably 3 or 4, most preferably 4.

[0108] If the linker is a peptide linker, as is preferred, then the first or last amino acid of the peptide is linked to the first or last amino acid of the peptide linker via a peptide bond.

[0109] If the peptide conjugate comprises a peptide linker and a PEG group, PEGylation is performed as described herein. N-terminal PEGylation is achieved, for example, using polyethylene glycol-N-hydroxysuccinimide (PEG-NHS). C-terminal PEGylation is achieved, for example, by Michael addition of polyethylene glycol maleimide to the thiol group of a terminal cysteine. Alternatively, C-terminal PEGylation can also be achieved by adding polyethylene glycol maleimide to the OH group of any terminal amino acid.

[0110] Typically, such peptide linkers have a length of 1 to 200 amino acids, e.g. 1 to 100 amino acids, preferably 2 to 30 amino acids, more preferably 5 to 25 amino acids.

[0111] In various embodiments, the linker is selected from the following group: (I) (GGGGS) n with n = 1, 2, 3, or 4; (II) (G)6; (III) (G)8; (IV) (EAAAK) n with n = 1, 2, or 3; (V) A(EAAAK)4ALEA(EAAAK)4A; (VI) PAPAP; (VII) AEAAAKEAAAKA; and (VIII) (AP) n with n = 10-34.

[0112] In the context of the present invention, functional homologs of the aforementioned linker sequences are also suitable. “Functional homologs”, as used in this context, refers to sequences that are at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5%, 98.8%, 99.0%, 99.2%, 99.4% or 99.6% identical to the specified reference sequence and have its functionality, i.e. as a bond between peptides and / or peptide and PEG chain without compromising the advantageous properties of corresponding peptide conjugates as described and disclosed herein.

[0113] Preferred linkers according to the invention have one of the following amino acid sequences: • GGGGS (SEQ ID NO:29), • GGGGSGGGGS (SEQ ID NO:30), • GGGGSGGGGGSGGGGS (SEQ ID NO:31), • GGGGSGGGGSGGGGSGGGGS (SEQ ID NO:32), • GGGGGGGG (SEQ ID NO:33), • GGGGGG (SEQ ID NO:34), • EAAAK (SEQ ID NO:35), • EAAAKEAAAK (SEQ ID NO:36), • EAAAKEAAAKEAAAK (SEQ ID NO:37), • AEAAAKEAAAKEAAAKEAAAKALEAEAAAKEAAAKEAAAKEAAAKA (SEQ ID NO:38), • PAPAP (SEQ ID NO:39) or • AEAAAKEAAAKA (SEQ ID NO:40).

[0114] Particularly preferred is the linker with the following amino acid sequence: • GGGGSGGGGSGGGGS (SEQ ID NO:31) or • EAAAKEAAAKEAAAK (SEQ ID NO:37).

[0115] In preferred embodiments, the peptide conjugate has the following structure in N- to C-terminal orientation: (i) Z1Z3Z4Z5Z7, (ii) Z2Z3Z4Z5Z6, (iii) Z1Z3Z4Z5Z6, (iv) Z2Z3Z4Z5Z7, (V) Z1Z3Z4, (vi) Z2Z3Z4, (vii) Z4Z5Z7, or (viii) Z4Z5Z6,wherein Z4 is a peptide, preferably a textile binding peptide, selected from (A) a peptide with the following amino acid sequence: (C)mX1X2X3(X4)nX5(C)o, where C is the amino acid cysteine, where m+o = 0 or 1; where X1 is a positively charged amino acid, preferably R or K, more preferably R, X2 and X3 are uncharged amino acids, preferably A, L, S, I, M or Q, more preferably A, S, I or L, particularly preferably A or L, each X4 independently of one another is any amino acid, preferably with the exception of P, more preferably with the exception of P and G, X5 is any positively charged or uncharged amino acid, preferably R or an uncharged amino acid, more preferably Q, A or L, particularly preferably A or L, m and o are 0 or 1, where n is an integer from 0 to 46, preferably 6 to 20, more preferably 6 to 12, particularly preferably 8 to 12, (B) a peptide having an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NO:1-27, where s = 1; where Z1 and Z7 are independently -(C2H4O) k where k = 5-100, preferably k = 20-85, preferably k = 30-75, particularly preferably k = 40-60, p and w are 0 or 1 and p+w = 0 to 2; wherein Z2 and Z6 are independently a peptide, preferably a textile-non-binding peptide, which has an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with the amino acid sequence given in SEQ ID NO:28, wherein q and v are 0 or 1 and q+v = 0 to 2; where Z3 and Z5 are peptide linkers, where the peptide linker is selected from the group consisting of (I) (GGGGS) n with n = 1, 2, 3, or 4; (II) (G)6; (III) (G)8; (IV) (EAAAK) n with n = 1, 2, or 3; (V) A(EAAAK)4ALEA(EAAAK)4A; (VI) PAPAP; (VII) AEAAAKEAAAKA; and (VIII) (AP) n with n = 10-34; existing group is selected, r and t are 0 or 1 and r+t = 0 to 2; where p+q+r+t+v+w = 2 to 6, preferably 3 to 5, particularly preferably 3 or 4, most preferably 4.

[0116] In preferred embodiments, the peptide conjugate has the following structure in N- to C-terminal orientation: (i) PEG - linker (I) - textile binding peptide - linker (I) - PEG, (ii) textile-nonbinding peptide - linker (I) - textile-binding peptide - linker (I) - textile-nonbinding peptide, (iii) PEG - linker (I) - textile-binding peptide - linker (I) - textile-non-binding peptide, (iv) textile-nonbinding peptide - linker (I) - textile-binding peptide - linker (I) - PEG chain, (v) PEG - Linker (I) - textile binding peptide, (vi) textile-nonbinding peptide - linker (I) - textile-binding peptide, (vii) textile binding peptide - linker (I) - PEG, (viii) textile-binding peptide - linker (I) - textile-non-binding peptide, (ix) PEG - Linker (II) - textile binding peptide - Linker (II) - PEG, (x) textile-nonbinding peptide - linker (II) - textile-binding peptide - linker (II) - textile-nonbinding peptide, (xi) PEG - Linker (II) - textile-binding peptide - Linker (II) - textile-non-binding peptide, (xii) textile-nonbinding peptide - linker (II) - textile-binding peptide - linker (II) - PEG, (xiii) PEG - linker (II) - textile binding peptide, (xiv) textile-nonbinding peptide - linker (II) - textile-binding peptide, (xv) textile-binding peptide - linker (II) - PEG, (xvi) textile-binding peptide - linker (II) - textile-non-binding peptide, (xvii) PEG - Linker (III) - textile binding peptide - Linker (III) - PEG, (xviii) textile-nonbinding peptide - linker (III) - textile-binding peptide - linker (III) - textile-nonbinding peptide, (xix) PEG - linker (III) - textile-binding peptide - linker (III) - textile-non-binding peptide, (xx) textile-nonbinding peptide - linker (III) - textile-binding peptide - linker (III) - PEG, (xxi) PEG - Linker (III) - textile binding peptide, (xxii) textile-nonbinding peptide - linker (III) - textile-binding peptide, (xxiii) textile binding peptide - linker (III) - PEG, (xxiv) textile-binding peptide - linker (III) - textile-non-binding peptide, (xxv) PEG - Linker (IV) - textile binding peptide - Linker (IV) - PEG, (xxvi) textile-nonbinding peptide - linker (IV) - textile-binding peptide - linker (IV) - textile-nonbinding peptide, (xxvii) PEG - linker (IV) - textile-binding peptide - linker (IV) - textile-non-binding peptide, (xxviii) textile-nonbinding peptide - linker (IV) - textile-binding peptide - linker (IV) - PEG, (xxix) PEG - Linker (IV) - textile binding peptide, (xxx) textile-nonbinding peptide - linker (IV) - textile-binding peptide, (xxxi) textile-binding peptide - linker (IV) - PEG, (xxxii) textile-binding peptide - linker (IV) - textile-non-binding peptide, (xxxiii) PEG - linker (V) - textile binding peptide - linker (V) - PEG, (xxxiv) textile-nonbinding peptide - linker (V) - textile-binding peptide - linker (V) - textile-nonbinding peptide, (xxxv) PEG - Linker (V) - textile-binding peptide - Linker (V) - textile-non-binding peptide, (xxxvi) textile-nonbinding peptide - linker (V) - textile-binding peptide - linker (V) - PEG, (xxxvii) PEG - linker (V) - textile binding peptide, (xxxviii) textile-nonbinding peptide - linker (V) - textile-binding peptide, (xxxix) textile-binding peptide - linker (V) - PEG, (xl) textile-binding peptide - linker (V) - textile-non-binding peptide, (xli) PEG - linker (VI) - textile binding peptide - linker (VI) - PEG, (xlii) textile-nonbinding peptide - linker (VI) - textile-binding peptide - linker (VI) - textile-nonbinding peptide, (xIiii) PEG - Linker (VI) - textile-binding peptide - Linker (VI) - textile-non-binding peptide, (xliv)textile non-binding peptide - linker (VI) - textile binding peptide - linker (VI) - PEG, (xlv) PEG - linker (VI) - textile binding peptide, (xlvi) textile-nonbinding peptide - linker (VI) - textile-binding peptide, (xlvii) textile binding peptide - linker (VI) - PEG, (xlviii) textile-binding peptide - linker (VI) - textile-non-binding peptide, (xlix)PEG- Linker (VII) - textile binding peptide - Linker (VII) - PEG, (I) textile-nonbinding peptide - linker (VII) - textile-binding peptide - linker (VII) - textile-nonbinding peptide, (li) PEG - linker (VII) - textile-binding peptide - linker (VII) - textile-non-binding peptide, (iii) textilnichtbindendes Peptid - Linker (VII) - textilnichtbindendes Peptid - Linker (VII) - PEG, (Iiii) PEG- Linker (VII) - textile-binding peptide, (liv) textilnichtbindendes Peptid - Linker (VII) - textilnichtbindendes Peptid, (IV) textilbindendes Peptide - Linker (VII) - PEG-Kette, (Ivi) textilbindendes Peptid - Linker (VII) - textilnichtbindendes Peptid, (Ivii) PEG- Linker (VIII) - textile-binding peptide - Linker (VIII) - PEG, (Iviii) non-textile-binding peptide - linker (VIII) - non-textile-binding peptide - linker (VIII) - non-textile-binding peptide, (Iix) PEG- Linker (VIII) - textilbindendes Peptid - Linker (VIII) - textilnichtbindendes Peptid, (Ix) textilnichtbindendes Peptid - Linker (VIII) - textilnichtbindendes Peptid - Linker (VIII) - PEG, (Ixi) PEG - Linker (VIII) - textile-binding peptide, (Ixii) textilnichtbindendes Peptid - Linker (VIII) - textilnichtbindendes Peptid, (Ixiii) textile binding peptide - linker (VIII) - PEG, (Ixiv) textile-binding peptide - linker (VIII) - textile-nonbinding peptide, where PEG -(C2H4O) k where k = 5-100, preferably k = 20-85, preferably k = 30-75, particularly preferably k = 40-60; wherein the textile-binding peptide is a peptide selected from (A) a peptide with the following amino acid sequence: (C)mX1X2X3(X4)nX5(C)o, where X1 is a positively charged amino acid, preferably R or K, more preferably R, X2 and X3 are uncharged amino acids, preferably A, L, S, I, M or Q, more preferably A, S, I or L, particularly preferably A or L, each X4 independently of one another is any amino acid, preferably with the exception of P, more preferably with the exception of P and G, X5 is any positively charged or uncharged amino acid, preferably R or an uncharged amino acid, more preferably R, Q, A or L, particularly preferably R, A or L, m and o are 0 or 1, where m+o = 0 or 1, and n is an integer from 0 to 46, preferably 6 to 20, more preferably 6 to 12, particularly preferably 8 to 12; and / or (B) a peptide having an amino acid sequence which has at least 80%, and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with any of the amino acid sequences set forth in SEQ ID NO:1-27; wherein the textile non-binding peptide is a peptide having an amino acid sequence having at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with the amino acid sequence set out in SEQ ID NO:28.

[0117] In preferred embodiments, the linker is selected from: • GGGGS (SEQ ID NO:29), • GGGGSGGGGS (SEQ ID NO:30), • GGGGSGGGGGSGGGGS (SEQ ID NO:31), • GGGGSGGGGSGGGGSGGGGS (SEQ ID NO:32), • GGGGGGGG (SEQ ID NO:33), • GGGGGG (SEQ ID NO:34), • EAAAK (SEQ ID NO:35), • EAAAKEAAAK (SEQ ID NO:36), • EAAAKEAAAKEAAAK (SEQ ID NO:37), • AEAAAKEAAAKEAAAKEAAKEAAAAKEAAKEAAAAAKA (SEQ ID NO:38), • POTATO (SEQ ID NO:39) und • AEAAAKEAAAKA (SEQ ID NO:40); and / or other non-binding textiles from: • NGLLIPQFLVAS (SEQ ID NO:28); and / or other textile-binding Peptide listed from: • RALQALRALQALEAL (SEQ ID NO:1), • RALRALEALLEAL (SEQ ID NO:2), • STARTING UP (SEQ ID NO:3), • RALRALRALQALEAL (SEQ ID NO:4), • RALRALQALEAL (SEQ ID NO:5), • RALFEALQALFRALEAL (SEQ ID NO:6), • RALRALEALQALEA (SEQ ID NO:7), • RALFEAL FRALEALR (SEQ ID NO:8), • RAPEFRALEAL (SEQ ID NO:9), • RALEALFRALEAL (SEQ ID NO:10), • RALRALFEALEAL (SEQ ID NO:11), • RALEALFRALQALEAL (SEQ ID NO:12), • RALEALWRALQALEAL (SEQ ID NO:13), • RALEALWRALEAL (SEQ ID NO:14), • RALARALARALAQALA (SEQ ID NO:15), • RSIVTFSLRQNAQLA (SEQ ID NO:16), • RSIVTFSLRQNSEQA (SEQ ID NO:17), • GLHTSATNLYLH (SEQ ID NO:18), • QHSIRLLTIKKP (SEQ ID NO:19), • QQSIRIMTIKHP (SEQ ID NO:20), • WRHPRLRCGNLL (SEQ ID NO:21), • QKSRNRMTRTHP (SEQ ID NO:22), • SRARLFVVTYHK (SEQ ID NO:23), • HMISTMNAASRR (SEQ ID NO:24), • RSIVTFSLRQNR (SEQ ID NO:25), • RNTIRIRTIKHP (SEQ ID NO:26), and • RHSSTLRYRPLP (SEQ ID NO:27).

[0118] In particularly preferred embodiments, the linker is selected from: • GGGGS (SEQ ID NO:29), • GGGGSGGGGSGGGGS (SEQ ID NO:31) and • EAAAKEAAAKEAAAK (SEQ ID NO:37); and the textile non-binding peptide selected from: • NGLLIPQFLVAS (SEQ ID NO:28); and the textile binding peptide selected from: • RALQALRALQALEAL (SEQ ID NO:1), • RALRALRALEALEAL (SEQ ID NO:2), • RALRALRALQALQAL (SEQ ID NO:3), • RALRALRALQALEAL (SEQ ID NO:4), • RALRALQALEEALEAL (SEQ ID NO:5), • RALFEALQALFRALEAL (SEQ ID NO:6), • RALRALEALQALEA (SEQ ID NO:7), • RALFEALFRALEALR (SEQ ID NO:8), • RALFEALFRALEAL (SEQ ID NO:9), • RALEALFRALEAL (SEQ ID NO:10), • RALRALFEALEAL (SEQ ID NO:11), • RALEALFRALQALEAL (SEQ ID NO:12), • RALEALWRALQALEAL (SEQ ID NO:13), • RALEALWRALEAL (SEQ ID NO:14), • RALARALARALAQALA (SEQ ID NO:15), • RSIVTFSLRQNAQLA (SEQ ID NO:16), • RSIVTFSLRQNSEQA (SEQ ID NO:17), • GLHTSATNLYLH (SEQ ID NO:18), • QHSIRLLTIKKP (SEQ ID NO:19), • QQSIRIMTIKHP (SEQ ID NO:20), • WRHPRLRCGNLL (SEQ ID NO:21), • QKSRNRMTRTHP (SEQ ID NO:22), • SRARLFVVTYHK (SEQ ID NO:23), • HMISTMNAASRR (SEQ ID NO:24), • RSIVTFSLRQNR (SEQ ID NO:25), • RNTIRIRTIKHP (SEQ ID NO:26), and • RHSSTLRYRPLP (SEQ ID NO:27).

[0119] In particularly preferred embodiments, the linker is selected from: • GGGGS (SEQ ID NO:29); andthe textile-nonbinding peptide selected from: • NGLLIPQFLVAS (SEQ ID NO:28); and the textile binding peptide selected from: • RALQALRALQALEAL (SEQ ID NO:1), • RALRALQALEALEAL (SEQ ID NO:5), and • RSIVTFSLRQNR (SEQ ID NO:25).

[0120] In further preferred embodiments, the linker is selected from: • GGGGS (SEQ ID NO:29); andthe textile-nonbinding peptide selected from: • NGLLIPQFLVAS (SEQ ID NO:28); and the textile binding peptide selected from: • RALQALRALQALEAL (SEQ ID NO:1).

[0121] In further preferred embodiments, the linker is selected from: • GGGGS (SEQ ID NO:29); andthe textile-nonbinding peptide selected from: • NGLLIPQFLVAS (SEQ ID NO:28); and the textile binding peptide selected from: • RALRALQALEEALEAL (SEQ ID NO:5).

[0122] In further preferred embodiments, the linker is selected from: • GGGGS (SEQ ID NO:29); andthe textile-nonbinding peptide selected from: • NGLLIPQFLVAS (SEQ ID NO:28); and the textile binding peptide selected from: • RSIVTFSLRQNR (SEQ ID NO:25).

[0123] Particularly preferred peptide conjugates include: • (PEG)-GGGGS-RSIVTFSLRQNR-GGGGS-(PEG) (SEQ ID NO:41), • (PEG)-GGGGS-RALQALRALQALEAL-GGGGS-(PEG) (SEQ ID NO:42), • (PEG)-GGGGS-RALRALQALEEALEAL-GGGGS-(PEG) (SEQ ID NO:43), • NGLLIPQFLVAS-GGGGS-RSIVTFSLRQNR-GGGGS-NGLLIPQFLVAS (SEQ ID NO:44), • NGLLIPQFLVAS-GGGGS-RALQALRALQALEAL-GGGGS-NGLLIPQFLVAS (SEQ ID NO:45), und • NGLLIPQFLVAS-GGGGS-RALRALQALEALEAL-GGGGS-NGLLIPQFLVAS (SEQ ID NO:46).

[0124] The identity of nucleic acid or amino acid sequences is determined by sequence comparison. This sequence comparison is based on the BLAST algorithm, which is established and commonly used in the state of the art (see, for example, Altschul et al. (1990) Basic local alignment search tool, J. Mol. Biol., 215:403-410, and Altschul et al. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs, Nucleic Acids Res., 25:3389-3402) and is essentially achieved by matching similar sequences of nucleotides or amino acids in the nucleic acid or amino acid sequences to one another. A tabular assignment of the relevant positions is referred to as an alignment. Another algorithm available in the state of the art is the FASTA algorithm. Sequence comparisons (alignments), especially multiple sequence comparisons, are created using computer programs. Frequently used, for example, are the Clustal series (see e.g. Chenna et al.(2003) Multiple sequence alignment with the Clustal series of programs, Nucleic Acid Res., 31:3497-3500), T-Coffee (cf. e.g. Notredame et al. (2000) T-Coffee: A novel method for multiple sequence alignments, J. Mol. Biol., 302:205-217) or programs based on these programs or algorithms. Sequence comparisons (alignments) are also possible using the computer program Vector NTI® Suite 10.3 (Invitrogen Corporation, 1600 Faraday Avenue, Carlsbad, California, USA) with the specified standard parameters, whose AlignX module for sequence comparisons is based on ClustalW, or Clone Manager 10 (use of the BLOSUM 62 scoring matrix for sequence alignment at the amino acid level). Unless otherwise stated, the sequence identity stated herein is determined using the BLAST algorithm.

[0125] Such a comparison also allows a statement to be made about the similarity of the compared sequences to one another. This is usually expressed as percent identity, i.e. the proportion of identical nucleotides or amino acid residues at the same positions or corresponding positions in an alignment. The broader term homology in amino acid sequences includes conserved amino acid substitutions, i.e. amino acids with similar chemical activity, since these usually exert similar chemical activities within the protein. Therefore, the similarity of the compared sequences can also be expressed as percent homology or percent similarity. Identity and / or homology statements can be made for entire polypeptides or genes, or just for individual regions. Homologous or identical regions of different nucleic acid or amino acid sequences are therefore defined by similarities in the sequences.Such regions often exhibit identical functions. They can be small and comprise only a few nucleotides or amino acids. Such small regions often perform essential functions for the overall activity of the protein. It may therefore be useful to refer sequence matches only to individual, possibly small regions. Unless otherwise stated, however, statements of identity or homology in this application refer to the entire length of the respective nucleic acid or amino acid sequence.

[0126] The peptide or protein concentration can be determined using known methods, e.g., the BCA method (bicinchoninic acid; 2,2'-biquinolyl-4,4'-dicarboxylic acid) or the biuret method (Gornall et al., J. Biol. Chem., 1948, 177:751-766). Those skilled in the art of peptide and protein technology are familiar with a variety of suitable methods for determining peptide or protein concentration that can be applied within the scope of this invention.

[0127] Peptides according to the invention may contain amino acid modifications, particularly amino acid substitutions, insertions, or deletions. Such peptides are further developed, for example, through targeted genetic modification, ie, through mutagenesis techniques, and optimized for specific applications or with regard to specific properties (e.g., with regard to their stability, binding, etc.).

[0128] For example, targeted mutations such as substitutions, insertions, or deletions can be introduced into known molecules to alter specific properties. For this purpose, the surface charges and / or the isoelectric point of the molecules, and thus their interactions with a surface, can be altered. For example, the net charge of the peptides can be altered to influence substrate binding. Alternatively or additionally, one or more corresponding mutations can increase, for example, the stability or adsorption of the peptide. Advantageous properties of individual mutations, such as individual substitutions, can complement each other.

[0129] Thus, the invention also encompasses peptides which are characterized in that they are obtainable from a peptide as described above as a starting molecule, e.g. from a molecule having one of the amino acid sequences according to SEQ ID NO:1-46, on which e.g. one or more amino acid substitutions, including single or multiple conservative amino acid substitutions, have been carried out, wherein the resulting peptide has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% and less than 100% sequence identity with one of the amino acid sequences according to SEQ ID NO:1-28.

[0130] The term "conservative amino acid substitution" means the exchange (substitution) of one amino acid residue for another amino acid residue, whereby this exchange does not lead to a change in the polarity or charge at the position of the exchanged amino acid, e.g., the exchange of a non-polar amino acid residue for another non-polar amino acid residue. Conservative amino acid substitutions within the scope of the invention include, for example: G=A=S, I=V=L=M, D=E, N=Q, K=R, Y=F, S=T, G=A=I=V=L=M=Y=F=W=P=S=T. However, it may be preferred that such exchanges do not have glycine or tyrosine as the target amino acid, or, for example, an amino acid that has a low alpha-helix-forming potential.

[0131] In preferred embodiments, the peptide according to the invention can also be modified. Preferred modifications can include, for example, coupling the peptide with certain other molecules or chemical groups, e.g., organic (macro)molecules, e.g., via a covalent bond or a linker / spacer via a suitable amino acid of the chain and / or N- and / or C-terminal.

[0132] All of the above features and embodiments can be implemented individually or in any combination.

[0133] Furthermore, the peptide according to the invention can also be at least one subunit (module) of a larger peptide or polypeptide, where the polypeptide can comprise a multimer of the sequences described herein, e.g. 1 to 30 repeats, more preferably 2 to 15 repeats, particularly preferably 2 to 10 repeats, e.g. 2, 3, 4, 5 or 6 repeats of the peptide. The polypeptide can comprise or consist of such multimers. The term "polypeptide" in this context refers in particular to peptides that comprise 100 or more amino acids. The term "larger peptides" preferably refers to peptides with at least 40 amino acids, unless otherwise described.

[0134] In various embodiments, the peptide is a peptide or polypeptide (multimer) comprising two or more of the peptides as described herein. In various embodiments, the two or more peptides can be linked to one another by at least one spacer; preferably, the at least one spacer comprises or consists of 1 to 10 amino acid residues, in particular 2, 3, or 4 amino acid residues, preferably selected from the group consisting of G, P, I, A, and S or combinations thereof, in particular GPI or GAS. In such embodiments, the individual peptides are optionally linked to one another linearly via peptide bonds, optionally also via a spacer.

[0135] The peptides described herein can, in various embodiments, be chemically synthesized and / or produced recombinantly by protein design. Short peptides are now easily synthesized, e.g., using solid-phase synthesis such as the Merrifield solid-phase synthesis. Longer peptides and polypeptides, on the other hand, are often also produced recombinantly in the host organism, e.g., in bacteria or yeast.

[0136] It is preferable to produce the peptides and / or peptide conjugates according to the invention using recombinant methods. This refers to all genetic engineering or microbiological methods based on the introduction of the genes for the peptides of interest into a host organism suitable for production and their transcribing and translation by the host organism (collectively referred to as biotechnological methods within the scope of this invention).

[0137] The peptides and / or peptide conjugates according to the invention are particularly preferably produced as polypeptides (multimers) and subsequently cleaved into the functional peptides and / or peptide conjugates. Very particularly preferred multimers comprise 1 to 30 peptide units (each according to the invention), each separated from one another by spacers of 1 to 10 amino acids in length (e.g., 1, 2, 3, or 4 amino acids). Alternatively, the spacers can also be or comprise cleavage sites for specific proteases / peptidases, in particular endopeptidases, or form such a cleavage site together with parts of the peptide.

[0138] Using methods commonly known today, such as chemical synthesis or the polymerase chain reaction (PCR) in conjunction with standard molecular biological and / or protein chemical methods, a person skilled in the art can produce the corresponding nucleic acids, including complete genes, based on known DNA and / or amino acid sequences. Such methods are known, for example, from Sambrook, J., Fritsch, EF and Maniatis, T. 2001. Molecular cloning: a laboratory manual, 3rd Edition. Cold Spring Laboratory Press.

[0139] In particularly preferred embodiments, the peptide and / or peptide conjugate described herein is produced by biotechnological methods as described above. Detergents or cleaning agents

[0140] Preferably, the at least one peptide and / or peptide conjugate according to the invention is suitable for adhesion and / or binding to textiles, as described herein.

[0141] It is particularly preferred that the peptide and / or peptide conjugate according to the invention, especially when used in washing or cleaning agents according to the invention, achieves a soil-repellent and / or soil-removing effect, particularly through binding and / or adhesion to textiles, preferably polyester-containing textiles, particularly preferably polyester / cotton blends. Thus, the washing or cleaning agent is preferably used as a detergent in a washing process, especially in machine or hand washing.

[0142] In various embodiments, the peptide and / or peptide conjugate described herein is used in the washing or cleaning agent according to the invention, without being limited thereto, in a concentration of 0.00001 to 5 wt.%, e.g. in a concentration of 0.0001 to 2 wt.% or 0.001 to 1 wt.%.

[0143] In preferred embodiments, the washing or cleaning agent is a textile detergent.

[0144] The washing or cleaning agent according to the invention is particularly suitable for use on textiles made of plastic and / or with a plastic content (mixed fabric) and / or made of a natural fiber such as cotton.The textile preferably comprises or consists of polyester (PES), polyethylene (PE), polypropylene (PP), polyurethane (PU), polystyrene (PS), polyvinyl chloride (PVC), polycarbonate (PC), polyamide (PA), polyphenylene ether, polyphenylene sulfide, polyoxymethylene (POM), polymethyl methacrylate (PMA), polyethylene terephthalate (PET), polybutylene terephthalate (PBT), polytetrafluoroethylene (PTFE), polyhydroxyalkanoate (PHA), polyhydroxybutyrate (PHB), polyimide (PI), polylactide (PLA), polyvinylidene fluoride (PVDF), polyether ketone (PEK), and / or copolymers or a blended fabric thereof, even more preferably polyester (PES), polyethylene (PE), polypropylene (PP), polystyrene (PS), copolymers or blended fabrics thereof, preferably a cotton / polyester blend with a polyester content of at least 10%, preferably at least 20%, more preferably at least 30%, even more preferably at least 40%, even more preferably at least 50%, even more preferably at least 60%, e.g.65%, or pure polyester or copolymers thereof.

[0145] The term "mixture" or "mixed fabric" refers to textiles with a plastic content, preferably textiles made of at least one natural fiber and at least one plastic fiber (plastic content). In particular, the mixture or mixed fabric consists of cotton and at least one plastic, in particular polyester. In preferred embodiments, a textile with a plastic content or a plastic mixture or mixed fabric has a plastic content of at least 10%, more preferably at least 20%, even more preferably at least 30%, even more preferably at least 40%, even more preferably at least 50%, even more preferably at least 60%, e.g., 65%.

[0146] The compositions of the washing or cleaning agents according to the invention, as well as the amounts of the ingredients, depend on the respective intended use and the trained specialist is generally familiar with suitable dosages of these components and can obtain these from the relevant specialist literature.

[0147] The washing and cleaning agents according to the invention include all conceivable types of washing or cleaning agents, both concentrated and undiluted, for use on a commercial scale, in washing machines or for hand washing or cleaning. These include, for example, washing agents for textiles, carpets, or natural fibers, for which the term "washing agent" is used. These also include, for example, dishwashing detergents for dishwashers (machine dishwashing detergents) or manual dishwashing detergents or cleaners for hard surfaces such as metal, glass, porcelain, ceramics, tiles, stone, painted surfaces, plastics, wood, or leather, for which the term "cleaning agent" is used. Thus, in addition to manual and machine dishwashing detergents, scouring agents, glass cleaners, toilet air fresheners, etc.The washing and cleaning agents within the scope of the invention also include washing aids which are added to the actual washing agent during manual or machine washing of textiles in order to achieve an additional effect. Furthermore, washing and cleaning agents within the scope of the invention also include textile pre- and post-treatment agents, i.e. agents with which the item of laundry is brought into contact before the actual washing, e.g. to dissolve stubborn soiling, and also agents which, in a step following the actual textile washing, impart further desirable properties to the laundry such as a pleasant feel, freedom from creasing or low static charge. The latter agents include, among others, fabric softeners. This also includes agents for use in (semi-)automated washing or cleaning systems such as robot mops or wet vacuum cleaners.

[0148] The detergents or cleaning agents according to the invention, which can be in powdered or granular solid form, in compacted or recompacted particle form, as homogeneous solutions or suspensions, can contain all known ingredients commonly used in such agents. The agents according to the invention can contain, in particular, surfactants, builders, complexing agents, polymers, glass corrosion inhibitors, corrosion inhibitors, bleaching agents such as peroxygen compounds, bleach activators or bleach catalysts, water-miscible organic solvents, enzyme stabilizers, sequestering agents, electrolytes, pH regulators, and / or other auxiliaries such as optical brighteners, graying inhibitors, dye transfer inhibitors, foam regulators, as well as dyes and fragrances.Advantageous ingredients of the compositions according to the invention are disclosed in the international patent application WO 2009 / 121725, beginning on page 5, penultimate paragraph, and ending on page 13 after the second paragraph. This disclosure is expressly incorporated by reference, and the disclosure content therein is incorporated into the present patent application.

[0149] Further embodiments of the invention include all solid, powdered, liquid, gel-like, or pasty dosage forms of agents according to the invention, which may optionally also consist of multiple phases and may be in compressed or uncompressed form. The agent may be in the form of a free-flowing powder, in particular with a bulk density of 300 g / l to 1200 g / l, in particular 500 g / l to 900 g / l or 600 g / l to 850 g / l. Solid dosage forms of the agent also include extrudates, granules, tablets, or pouches. Alternatively, the agent may also be liquid, gel-like, or pasty, e.g., in the form of a non-aqueous liquid detergent or a non-aqueous paste, or in the form of an aqueous liquid detergent or a water-containing paste. Liquid agents are generally preferred. Furthermore, the agent may be in the form of a one-component system. Such agents consist of one phase. Alternatively, an agent may also consist of multiple phases.Such a remedy is therefore divided into several components.

[0150] In a preferred embodiment, the agent according to the invention is a textile detergent.

[0151] In a preferred embodiment, the agent according to the invention is a liquid textile detergent.

[0152] In a preferred embodiment, the agent according to the invention is a solid textile detergent.

[0153] Multiphase formulations are not preferred in the context of this invention, but are not excluded.

[0154] The viscosity of the liquid washing or cleaning agents at 20°C is preferably 5 to 100,000 mPa s, more preferably 10 to 5,000 mPa s, even more preferably 10 to 200 mPa s, measured with a Brookfield rotational viscometer of the LVT or LVDV-II+ type with a small sample adapter at a speed of 30 min -1The Brookfield spindle used as the measuring body should be selected so that the torque is within a favorable range and the measuring range is not exceeded. In this context, spindle 31 is preferred, and – if necessary for viscosities above approximately 240 mPa s – spindle 25 is preferred.

[0155] In a preferred embodiment, the agent according to the invention is a pre-portioned textile detergent, in particular a detergent portion unit comprising a detergent preparation according to the invention and a water-soluble film which completely encloses the detergent preparation. The water-soluble film in which the detergent preparation is packaged can comprise one or more structurally different water-soluble polymer(s). Particularly suitable as water-soluble polymer(s) are polymers from the group of (optionally acetalized) polyvinyl alcohols (PVAL) and their copolymers. Water-soluble films are preferably based on a polyvinyl alcohol or a polyvinyl alcohol copolymer whose molecular weight is in the range from 10,000 to 1,000,000 g / mol, preferably from 20,000 to 500,000 g / mol, particularly preferably from 30,000 to 100,000 g / mol and in particular from 40,000 to 80,000 g / mol. Suitable water-soluble films for use include:sold by MonoSol LLC, for example, under the designations M8630, M8720, M8310, C8400, or M8900. Also suitable are films named Solublon® PT, Solublon® GA, Solublon® KC, or Solublon® KL from Aicello Chemical Europe GmbH, or the VF-HP films from Kuraray.

[0156] When the agents according to the invention are in liquid form, they preferably contain, based on their total weight, more than 40% by weight, preferably 50 to 90% by weight and particularly preferably 60 to 80% by weight of water.

[0157] The agents according to the invention may contain one or more surfactants, with particular preference being given to anionic surfactants, nonionic surfactants, and mixtures thereof, but cationic, zwitterionic, and / or amphoteric surfactants may also be included. The agents preferably contain 5 to 70 wt.%, more preferably 35 to 60 wt.%, and more preferably 40 to 55 wt.% of surfactant.

[0158] Suitable anionic surfactants are, in particular, soaps and those containing sulfate or sulfonate groups with preferably alkali ions as cations. Suitable soaps are preferably the alkali salts of saturated or unsaturated C 12-18 -fatty acids. Such fatty acids can also be used in a form that is not completely neutralized. Useful sulfate-type surfactants include the salts of the sulfuric acid monoesters of C 12-18 -fatty alcohols and the sulfation products of the non-ionic surfactants mentioned with a low degree of ethoxylation. Suitable sulfonate-type surfactants include, for example, C 9-14 -Alkyl benzene sulfonates, alkane sulfonates derived from C 12-18 -alkanes, e.g. by sulfochlorination or sulfoxidation with subsequent hydrolysis or neutralization, C 12-18-Olefinsulfonates, which are formed by reacting corresponding monoolefins with sulfur trioxide, mixtures of alkene and hydroxyalkanesulfonates, disulfonates, such as those obtained from C 12-18 -Monoolefins with terminal or internal double bonds by sulfonation with gaseous sulfur trioxide and subsequent alkaline or acidic hydrolysis of the sulfonation products, as well as α-sulfofatty acid esters (ester sulfonates) which are formed during the sulfonation of fatty acid methyl or ethyl esters, e.g. α-sulfonated methyl esters of hydrogenated coconut, palm kernel or tallow fatty acids.

[0159] The agent preferably contains 2 to 55 wt.%, preferably 3 to 35 wt.%, of anionic surfactant. Most preferably, the agent contains 3 to 25 wt.% alkylbenzenesulfonate. In addition, the agent may preferably contain other anionic surfactants, especially alkyl ether sulfates, as well as nonionic surfactants, especially fatty alcohol alkoxylates. These can then make up the remainder of the surfactants.

[0160] Suitable alkylbenzenesulfonates are preferably selected from linear or branched alkylbenzenesulfonates of the formula: where R' and R'' are independently H or alkyl and together contain 6 to 19, preferably 7 to 15, and especially 9 to 13 carbon atoms. A particularly preferred representative is sodium dodecylbenzylsulfonate.

[0161] Alk(en)yl sulfates are the alkali metal and especially the sodium salts of the sulfuric acid half esters of C 12-18-Fatty alcohols, e.g. from coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl or stearyl alcohol or the C 10-20 -Oxo alcohols and those half esters of secondary alcohols of these chain lengths are preferred. Also preferred are alk(en)yl sulfates of the stated chain length, which contain a synthetic, petrochemically produced straight-chain alkyl radical, which have a degradation behavior similar to that of the corresponding compounds based on oleochemical raw materials. For washing purposes, the C 12-16 -alkyl sulfates and C 12-15 -alkyl sulfates and C 14-15 -Alkyl sulfates are preferred.

[0162] The sulfuric acid monoesters of the straight-chain or branched C ethoxylated with 1 to 6 moles of ethylene oxide 7-21 -alcohols, such as 2-methyl-branched C 9-11 -alcohols with an average of 3.5 moles of ethylene oxide (EO) or C 12-18 -Fatty alcohols with 1 to 4 EO are suitable.

[0163] Suitable alkyl ether sulfates are, for example, compounds of the formula R 1 -O-(AO) n -SO3 - X + .

[0164] In this formula, R 1 represents a linear or branched, substituted or unsubstituted alkyl radical, preferably a linear, unsubstituted alkyl radical, particularly preferably a fatty alcohol radical. Preferred radicals R 1 are selected from decyl, undecyl, dodecyl, tridecyl, tetradecyl, pentadecyl, hexadecyl, heptadecyl, octadecyl, nonadecyl, eicosyl radicals and mixtures thereof, with the representatives having an even number of carbon atoms being preferred. Particularly preferred radicals R 1 are derived from C 12-18 -fatty alcohols, e.g. coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl or stearyl alcohol or C 10-20-oxo alcohols. AO stands for an ethylene oxide (EO) or propylene oxide (PO) group, preferably an ethylene oxide group. The index n stands for an integer from 1 to 50, preferably from 1 to 20, and in particular from 2 to 10. Most preferably, n stands for the numbers 2, 3, 4, 5, 6, 7, or 8. X + stands for a monovalent cation or the n-th part of an n-valent cation, preferably the alkali metal ions and among them Na + or K + , where Na + is highly preferred. Other cations X + can be selected from NH4 + , ½ Zn 2+ , ½ mg 2+ , ½ Ca 2+ , ½ month 2+ and their mixtures.

[0165] In various embodiments, the alkyl ether sulfate can be selected from fatty alcohol ether sulfates of the formula with k = 11 to 19, n = 2, 3, 4, 5, 6, 7 or 8. Very particularly preferred representatives are Na-C 12 - 14Fatty alcohol ether sulfates with 2 EO (k = 11-13, n = 2). The stated degree of ethoxylation represents a statistical mean, which can be a whole or fractional number for a specific product. The stated degrees of alkoxylation represent statistical mean, which can be a whole or fractional number for a specific product. Preferred alkoxylates / ethoxylates exhibit a narrow homolog distribution (narrow range ethoxylates, NRE).

[0166] It has proven beneficial for cold-wash performance if the detergents also contain soap(s). Preferred detergents are therefore characterized by the presence of soap(s). Suitable soaps include saturated fatty acid soaps, such as the salts of lauric acid, myristic acid, palmitic acid, stearic acid, hydrogenated erucic acid, and behenic acid, as well as, in particular, soap mixtures derived from natural fatty acids, e.g., coconut, palm kernel, or tallow fatty acids.

[0167] Suitable nonionic surfactants are, in particular, alkyl glycosides and ethoxylation and / or propoxylation products of alkyl glycosides or linear or branched alcohols, each containing 8 to about 18 carbon atoms in the alkyl moiety and 3 to 20, preferably 4 to 10, alkyl ether groups. Furthermore, corresponding ethoxylation and / or propoxylation products of N-alkylamines, vicinal diols, fatty acid esters, and fatty acid amides, which correspond to the aforementioned long-chain alcohol derivatives with regard to the alkyl moiety, as well as of alkylphenols with 5 to 12 carbon atoms in the alkyl radical, are also suitable.

[0168] Nonionic surfactants used are preferably alkoxylated, advantageously ethoxylated, especially primary alcohols with preferably 8 to 18 C atoms and an average of 1 to 12 moles of ethylene oxide (EO) per mole of alcohol, in which the alcohol radical can be linear or preferably methyl-branched in the 2-position or can contain linear and methyl-branched radicals in a mixture, as is usually the case in oxo alcohol radicals. However, alcohol ethoxylates with linear radicals from alcohols of native origin with 12 to 18 C atoms, e.g., from coconut, palm, tallow, or oleyl alcohol, and an average of 2 to 8 EO per mole of alcohol are particularly preferred. Preferred ethoxylated alcohols include, for example, C 12-14 -Alcohols with 3 EO or 4 EO, C 9-11 -Alcohol with 7 EO, C 13-15 -Alcohols with 3 EO, 5 EO, 7 EO or 8 EO, C 12-18 -Alcohols with 3 EO, 5 EO or 7 EO and mixtures of these, such as mixtures of C 12-14 -Alcohol with 3 EO and C12 - 18 Alcohol with 5 EO. The stated degrees of ethoxylation represent statistical averages, which can be a whole or fractional number for a specific product. Preferred alcohol ethoxylates have a narrow homolog distribution (narrow range ethoxylates, NRE). In addition to these nonionic surfactants, fatty alcohols with more than 12 EO can also be used. Examples include tallow fatty alcohol with 14 EO, 25 EO, 30 EO, or 40 EO.

[0169] Another class of preferably used nonionic surfactants, which are used either as the sole nonionic surfactant or in combination with other nonionic surfactants, are alkoxylated, preferably ethoxylated or ethoxylated and propoxylated fatty acid alkyl esters, preferably having 1 to 4 carbon atoms in the alkyl chain, in particular fatty acid methyl esters.

[0170] Another class of nonionic surfactants that can be used advantageously are alkyl polyglycosides (APG). Suitable alkyl polyglycosides satisfy the general formula RO(G) z , in which R represents a linear or branched, in particular 2-methyl-branched, saturated or unsaturated, aliphatic radical having 8 to 22, preferably 12 to 18, carbon atoms, and G represents a glycose unit having 5 or 6 carbon atoms, preferably glucose. The degree of glycosidation z is between 1 and 4, preferably between 1 and 2, and in particular between 1.1 and 1.4. Linear alkyl polyglycosides are preferred, i.e., alkyl polyglycosides in which the polyglycosyl radical is a glucose radical and the alkyl radical is an n-alkyl radical.

[0171] Nonionic surfactants of the amine oxide type, e.g., N-cocoalkyl-N,N-dimethylamine oxide and N-tallowalkyl-N,N-dihydroxyethylamine oxide, and fatty acid alkanolamides may also be suitable. The amount of these nonionic surfactants is preferably no more than that of the ethoxylated fatty alcohols, in particular no more than half that amount.

[0172] Suitable amphoteric surfactants are, for example, betaines of the formula (R iii )(R iv Y)(R v )N + CH2COO - , in the R iii an alkyl radical having 8 to 25, preferably 10 to 21 carbon atoms, optionally interrupted by heteroatoms or heteroatom groups, and R iv and R v identical or different alkyl radicals having 1 to 3 carbon atoms, in particular C 10 - 18 -Alkyldimethylcarboxymethylbetaine and C 11 - 17 -Alkylamidopropyldimethylcarboxymethylbetaine.

[0173] Suitable cationic surfactants include the quaternary ammonium compounds of the formula (R vi )(R vii )(R viii )(R ix )N + X - , in the R vi to R ix represents four identical or different, in particular two long- and two short-chain, alkyl radicals and X -represent an anion, especially a halide ion, e.g., didecyldimethylammonium chloride, alkylbenzyldidecylammonium chloride, and mixtures thereof. Other suitable cationic surfactants are quaternary surface-active compounds, especially those with a sulfonium, phosphonium, iodonium, or arsonium group, which are also known as antimicrobial agents. By using quaternary surface-active compounds with antimicrobial activity, the agent can be given an antimicrobial effect or its existing antimicrobial effect, possibly due to other ingredients, can be improved.

[0174] A further preferred component of agents according to the invention are complexing agents. Particularly preferred complexing agents are phosphonates, provided their use is permitted by regulations. In addition to 1-hydroxyethane-1,1-diphosphonic acid, the complexing phosphonates include a number of different compounds, such as diethylenetriaminepenta(methylenephosphonic acid) (DTPMP). In this application, hydroxyalkane and aminoalkanephosphonates are particularly preferred. Among the hydroxyalkanephosphonates, 1-hydroxyethane-1,1-diphosphonate (HEDP) is of particular importance as a cobuilder. It is preferably used as the sodium salt, with the disodium salt being neutral and the tetrasodium salt being alkaline (pH 9). Suitable aminoalkanephosphonates are preferably ethylenediaminetetramethylenephosphonate (EDTMP), diethylenetriaminepentamethylenephosphonate (DTPMP), and their higher homologues. They are preferably used in the form of the neutral sodium salts, e.g.as the hexasodium salt of EDTMP or as the hepta- and octasodium salt of DTPMP. HEDP, a phosphonate builder, is preferred. Aminoalkanephosphonates also possess pronounced heavy metal binding capacity.

[0175] Accordingly, it may be preferable, particularly if the agents also contain bleach, to use aminoalkanephosphonates, in particular DTPMP, or mixtures of the phosphonates mentioned. A preferred agent within the scope of this application contains one or more phosphonate(s) from the group consisting of aminotrimethylenephosphonic acid (ATMP) and / or its salts; ethylenediaminetetra(methylenephosphonic acid) (EDTMP) and / or its salts; diethylenetriaminepenta(methylenephosphonic acid) (DTPMP) and / or its salts; 1-hydroxyethane-1,1-diphosphonic acid (HEDP) and / or its salts; 2-phosphonobutane-1,2,4-tricarboxylic acid (PBTC) and / or its salts; hexamethylenediaminetetra(methylenephosphonic acid) (HDTMP) and / or its salts; Nitrilotri(methylenephosphonic acid) (NTMP) and / or its salts. Particularly preferred are agents containing 1-hydroxyethane-1,1-diphosphonic acid (HEDP) or diethylenetriaminepenta(methylenephosphonic acid) (DTPMP) as phosphonates.Of course, the agents according to the invention can contain two or more different phosphonates.

[0176] Preferred agents according to the invention are characterized in that the agent contains at least one complexing agent from the group of phosphonates, preferably 1-hydroxyethane-1,1-diphosphonate, wherein the weight fraction of the phosphonate in the total weight of the agent is preferably 0.1 and 8.0 wt.%, preferably 0.2 and 5.0 wt.%, more preferably 0.3 and 3.0 wt.% and particularly preferably 0.5-2.0 wt.%.

[0177] In further preferred embodiments, the washing and / or cleaning agents according to the invention are substantially free of phosphonate-containing compounds. "Substantially free of phosphonate-containing compounds" in this context means that the corresponding agents contain less than 2% by weight, preferably less than 1% by weight, more preferably less than 0.5% by weight, and particularly preferably less than 0.1% by weight, of phosphonate-containing compounds, based on the total weight of the agent. In particularly preferred embodiments, these agents are free of phosphonate-containing compounds.

[0178] The compositions according to the invention preferably further contain builders, preferably at least one water-soluble and / or water-insoluble, organic and / or inorganic builder. Builders include, in particular, silicates, carbonates, and organic cobuilders.

[0179] Organic cobuilders include, in particular, polycarboxylates / polycarboxylic acids, polymeric polycarboxylates, aspartic acid, polyacetals, dextrins, other organic cobuilders, and phosphonates. These classes of substances are described below. Organic cobuilder substances can, if desired, be present in amounts of up to 40 wt.%, in particular up to 25 wt.%, and preferably from 1 to 8 wt.%. Suitable organic builders include, for example, polycarboxylic acids, which can be used in the form of the free acid and / or their sodium salts. Polycarboxylic acids are understood to be carboxylic acids that carry more than one acid function.For example, these are citric acid, adipic acid, succinic acid, glutaric acid, malic acid, tartaric acid, maleic acid, fumaric acid, sugar acids and carboxymethyl inulins, monomeric and polymeric aminopolycarboxylic acids, in particular glycinediacetic acid, methylglycinediacetic acid, glutaminediacetic acid, nitrilotriacetic acid (NTA), iminodisuccinate such as ethylenediamine-N,N'-disuccinic acid and hydroxyiminodisuccinates, ethylenediaminetetraacetic acid and polyaspartic acid, polyphosphonic acids, in particular aminotris(methylenephosphonic acid), ethylenediaminetetrakis(methylenephosphonic acid), lysinetetra(methylenephosphonic acid) and 1-hydroxyethane-1,1-diphosphonic acid, polymeric hydroxy compounds such as dextrin and polymeric (poly)carboxylic acids, in particular by oxidation of polysaccharides orDextrin-accessible polycarboxylates, and / or polymeric acrylic acids, methacrylic acids, maleic acids, and copolymers thereof, which may also contain small amounts of polymerizable substances without carboxylic acid functionality. Such organic builder substances can, if desired, be present in amounts of up to 50% by weight, in particular up to 25% by weight, preferably from 10 to 20% by weight, and particularly preferably from 1 to 5% by weight. In addition to their builder effect, the free acids typically also have the property of an acidifying component and thus also serve to adjust a lower and milder pH value of agents. Particular mention should be made of citric acid, succinic acid, glutaric acid, adipic acid, gluconic acid, and any mixtures thereof. Citric acid or salts of citric acid are particularly preferably used as the builder substance.Further particularly preferred builders are selected from methylglycinediside acid (MGDA), glutamic acid diacetate (GLDA), aspartic acid diacetate (ASDA), hydroxyethyliminodiacetate (HEIDA), iminodisuccinate (IDS), ethylenediamine disuccinate (EDDS), carboxymethylinulin, and polyaspartate. In preferred embodiments, citric acid and / or citrate are used as the water-soluble, organic builder. Particular preference is given to using 0.5 to 25 wt.%, preferably 0.75 to 12.5 wt.%, more preferably 1 to 4 wt.% of citric acid and / or 0.5 to 25 wt.%, preferably 0.75 to 12.5 wt.%, more preferably 1 to 4 wt.% of citrate, preferably alkali metal citrate, even more preferably sodium citrate. Citric acid / citrate can each be used in the form of their hydrates, for example citric acid can be used in the form of the monohydrate, citrate in the form of trisodium citrate dihydrate.

[0180] Other suitable builders include polymeric polycarboxylates, for example the alkali metal salts of polyacrylic acid or polymethacrylic acid, e.g. those with a relative molecular mass of 500 to 70,000 g / mol. For the purposes of this application, the molecular masses stated for polymeric polycarboxylates are weight-average molecular masses Mw of the respective acid form, which were generally determined by gel permeation chromatography (GPC) using a UV detector. The measurement was carried out against an external polyacrylic acid standard, which, due to its structural similarity to the polymers investigated, provides realistic molecular weight values. These figures differ significantly from the molecular weight figures used when polystyrenesulfonic acids are used as the standard. The molecular masses measured against polystyrenesulfonic acids are generally significantly higher than the molecular masses stated in this application.Suitable polymers are, in particular, polyacrylates, which preferably have a molecular weight of 2000 to 20,000 g / mol. Due to their superior solubility, the short-chain polyacrylates, which have molecular weights of 2000 to 10,000 g / mol, and particularly preferably of 3000 to 5000 g / mol, may be preferred from this group. Copolymeric polycarboxylates are also suitable, in particular those of acrylic acid with methacrylic acid and of acrylic acid or methacrylic acid with maleic acid. Copolymers of acrylic acid with maleic acid, which contain 50 to 90 wt.% acrylic acid and 50 to 10 wt.% maleic acid, have proven particularly suitable. Their relative molecular weight, based on free acids, is generally 2000 to 70,000 g / mol, preferably 20,000 to 50,000 g / mol, and in particular 30,000 to 40,000 g / mol.

[0181] A solid composition according to the invention preferably contains at least one water-soluble and / or water-insoluble, organic and / or inorganic builder. The water-soluble organic builder substances include the above-mentioned organic builders.

[0182] In addition to the aforementioned water-soluble organic builders, the agents of the invention may also contain inorganic water-soluble builders. Suitable water-soluble inorganic builder materials include, in particular, alkali metal silicates, alkali metal carbonates, alkali metal hydrogen carbonates, alkali metal phosphates, and / or sesquicarbonates, which may be present in the form of their alkaline, neutral, or acidic sodium or potassium salts. Small amounts of calcium carbonates may also be present in solid textile detergents if desired. Suitable examples include water-soluble crystalline and / or amorphous alkali metal silicates. The alkali metal silicates usable as builders in the agents according to the invention preferably have a molar ratio of alkali metal oxide to SiO2 of less than 0.95, in particular of 1:1.1 to 1:12, and may be amorphous or crystalline.Preferred alkali silicates are sodium silicates, especially amorphous sodium silicates, with a molar ratio of Na2O:SiO2 of 1:2 to 1:2.8. Crystalline silicates, which can be present alone or in a mixture with amorphous silicates, are preferably crystalline layered silicates of the general formula Na2Si. x O 2x+1· y H2O, in which x, the so-called modulus, is a number from 1.9 to 22, in particular 1.9 to 4 and y is a number from 0 to 33 and preferred values ​​for x are 2, 3 or 4. Preferred crystalline layered silicates are those in which x in the general formula mentioned takes on the values ​​2 or 3. In particular, both β- and δ-sodium disilicates (Na2Si2O5 · y H2O) are preferred. Practically anhydrous crystalline alkali silicates produced from amorphous alkali silicates of the above general formula, in which x is a number from 1.9 to 2.1, can also be used in agents according to the invention. In a further embodiment of agents according to the invention, a crystalline sodium layered silicate with a modulus of 2 to 3 is used, such as can be produced from sand and soda. Crystalline sodium silicates with a modulus in the range of 1.9 to 3.5 are used in a further embodiment of the agents according to the invention.In agents containing both amorphous and crystalline alkali silicates, the weight ratio of amorphous alkali silicate to crystalline alkali silicate is preferably 1:2 to 2:1, and in particular 1:1 to 2:1. Crystalline layered silicates of the above-mentioned formula (I) are marketed by Clariant GmbH under the trade name Na-SKS, e.g., Na-SKS-1 (Na2Si). 22 O 45 · x H2O, Kenyaite), Na-SKS-2 (Na2Si 14 O 29 · × H2O, magadiite), Na-SKS-3 (Na2Si8O 17· × H2O) or Na-SKS-4 (Na2Si4O9 · × H2O, makatite). Of these, Na-SKS-5 (α-Na2Si2O5), Na-SKS-7 (β-Na2Si2O5, natrosilite), Na-SKS-9 (NaHSi2O5 · 3 H2O), Na-SKS-10 (NaHSi2O5 · 3 H2O, kanemite), Na-SKS-11 (t-Na2Si2O5) and Na-SKS-13 (NaHSi2O5), but especially Na-SKS-6 (δ-Na2Si2O5) are particularly suitable. In one embodiment of the inventive compositions, a granular compound of crystalline phyllosilicate and citrate, of crystalline phyllosilicate and the above-mentioned (co)polymeric polycarboxylic acid, or of alkali silicate and alkali carbonate is used, as is commercially available, for example, under the name Nabion® 15. Such water-soluble inorganic builder materials are preferably present in the inventive compositions in amounts of 1 to 20 wt.%, in particular 5 to 15 wt. Other important water-soluble inorganic builder substances are carbonates (and hydrocarbonates), in particular sodium carbonate, and phosphonic acids / phosphonates.

[0183] The agents according to the invention are preferably free of phosphate builders, ie they contain less than 1% by weight, preferably no deliberately added phosphate builder.

[0184] The agents may also contain water-insoluble builder substances. Water-insoluble inorganic builder materials used include, in particular, crystalline or amorphous, water-dispersible alkali aluminosilicates, in amounts of up to 50 wt.%, preferably not more than 40 wt.%, in particular from 3 to 20 wt.%, and particularly preferably from 1 to 15 wt.%. Among these, crystalline sodium aluminosilicates of detergent quality, in particular zeolite A, zeolite P, zeolite MAP, and optionally zeolite X, are preferred, alone or in mixtures, e.g., in the form of a co-crystallizate of zeolites A and X (Vegobond® AX, a commercial product of Condea Augusta SpA). Amounts close to the stated upper limit are preferably used in solid, particulate agents. Suitable aluminosilicates in particular do not have particles with a grain size of more than 30 µm and preferably consist of at least 80 wt.% of particles with a size of less than 10 µm.Their calcium binding capacity, which can be determined according to DE 2412837 A1, is generally in the range of 100 to 200 mg CaO per gram.

[0185] In addition to the previously described builders, the agent may contain cleaning-active polymers. The weight fraction of the cleaning-active polymers in the total weight of the agent according to the invention is preferably 0.1 to 20 wt.%, preferably 1.0 to 15 wt.%, and more preferably 2.0 to 12 wt.%.

[0186] Peroxygen compounds suitable for use in agents according to the invention include, in particular, organic peracids or peracidic salts of organic acids, such as phthalimidopercaproic acid, perbenzoic acid, or salts of diperdodecanedioic acid, hydrogen peroxide, and inorganic salts that release hydrogen peroxide under washing conditions, including perborate, percarbonate, persilicate, and / or persulfate such as caroate, as well as hydrogen peroxide inclusion compounds, such as H2O2-urea adducts. Hydrogen peroxide can also be produced with the aid of an enzymatic system, i.e., an oxidase and its substrate. If solid peroxygen compounds are to be used, they can be used in the form of powders or granules, which can also be coated in a manner known in principle.The peroxygen compounds can be added to the wash liquor as such or in the form of agents containing them, which in principle can contain all conventional washing, cleaning, or disinfectant ingredients. Particular preference is given to using alkali metal percarbonate or alkali metal perborate monohydrate. If an agent according to the invention contains peroxygen compounds, they are present in amounts of preferably up to 50 wt.%, in particular from 5 to 30 wt.%, more preferably from 0.1 to 20 wt.%.

[0187] Compounds that, under perhydrolysis conditions, yield aliphatic peroxocarboxylic acids with preferably 1 to 10 carbon atoms, especially 2 to 4 carbon atoms, and / or optionally substituted perbenzoic acid can be used as bleach activators in the detergents. Suitable substances are those containing O- and / or N-acyl groups with the stated number of carbon atoms and / or optionally substituted benzoyl groups. Preferred are multiply acylated alkylenediamines, in particular tetraacetylethylenediamine (TAED), acylated triazine derivatives, in particular 1,5-diacetyl-2,4-dioxohexahydro-1,3,5-triazine (DADHT), acylated glycolurils, in particular tetraacetylglycoluril (TAGU), N-acylimides, in particular N-nonanoylsuccinimide (NOSI), acylated phenolsulfonates or carboxylates or the sulfonic or carboxylic acids thereof, in particular nonanoyl or isononanoyloxybenzenesulfonate or laroyloxybenzenesulfonate (NOBS or iso-NOBS orLOBS), 4-(2-decanoyloxyethoxycarbonyloxy)-benzenesulfonate (DECOBS) or decanoyloxybenzoate (DOBA), carboxylic acid anhydrides, in particular phthalic anhydride, acylated polyhydric alcohols, in particular triacetin, ethylene glycol diacetate, 2,5-diacetoxy-2,5-dihydrofuran and enol esters as well as acetylated sorbitol and mannitol or their described mixtures (SORMAN), acylated sugar derivatives, in particular pentaacetylglucose (PAG), pentaacetylfructose, tetraacetylxylose and octaacetyllactose, acetylated, optionally N-alkylated glucamine and gluconolactone, N-acylated lactams, e.g. N-benzoylcaprolactam, nitriles from which perimidic acids are formed, in particular aminoacetonitrile derivatives with quaternized nitrogen atom, and / or Oxygen-transferring sulfonimines and / or acylhydrazones. Hydrophilically substituted acyl acetals and acyl lactams are also preferred. Combinations of conventional bleach activators can also be used.Such bleach activators can be present, particularly in the presence of the above-mentioned hydrogen peroxide-providing bleaching agents, in the usual amount range, preferably in amounts of 0.5 to 10 wt.%, in particular 1 to 8 wt.%, based on the total agent, but are preferably completely absent when percarboxylic acid is used as the sole bleaching agent.

[0188] In addition to the conventional bleach activators or instead of them, solid agents may also contain sulfonimines and / or bleach-enhancing transition metal salts or transition metal complexes as so-called bleach catalysts.

[0189] Suitable graying inhibitors or soil-release agents (soil-release polymers) are cellulose ethers, such as carboxymethylcellulose, methylcellulose, hydroxyalkylcelluloses, and cellulose mixed ethers, such as methylhydroxyethylcellulose, methylhydroxypropylcellulose, and methylcarboxymethylcellulose. Sodium carboxymethylcellulose, hydroxypropylmethylcellulose, and mixtures thereof, and optionally mixtures thereof with methylcellulose, are preferably used. Commonly used soil-release agents include copolyesters containing dicarboxylic acid units, alkylene glycol units, and polyalkylene glycol units. The proportion of graying inhibitors and / or soil-release agents in agents according to the invention generally does not exceed 2% by weight and is preferably 0.5 to 1.5% by weight, particularly preferably 0.5 to 2% by weight.

[0190] In various embodiments, the washing or cleaning agent according to the invention can contain, in addition to the at least one peptide and / or peptide conjugate as soil-release active ingredient, further soil-release active ingredients, preferably SRP polymers, although this embodiment is not preferred. These active ingredients can positively influence the ability of oil and grease to be washed out of textiles. This effect is particularly evident when a textile is soiled that has already been washed several times with an agent containing this oil- and grease-dissolving component. Preferred SRP active ingredients include, for example, non-ionic cellulose ethers such as methylcellulose and methylhydroxypropylcellulose with a proportion of methoxyl groups of 15 to 30 wt.% and of hydroxypropoxyl groups of 1 to 15 wt.%, in each case based on the non-ionic cellulose ether, as well as the polymers of phthalic acid and / or terephthalic acid orof their derivatives with monomeric and / or polymeric diols, in particular polymers of ethylene terephthalates and / or polyethylene glycol terephthalates or anionically and / or nonionically modified derivatives thereof. Such compounds are commercially available, for example, under the trade name Texcare®.

[0191] Typical soil release polymers for polyester-containing textiles can be based on copolymers of polyester and polyether, including terephthalate, e.g. polypropylene terephthalate. Examples of commercially available soil release polymers include the polymers sold by Rhodia under the trade name Repel-O-Tex, such as Repel-O-Tex SRP 4, Repel-O-Tex SRP 6, Repel-O-Tex PF, Repel-O-Tex PF 594; the polymers sold by BASF under the trade name Sokalan, such as Sokalan SR 100; the polymers sold by Sasol under the trade name Marloquest SL; the polymers sold by Clariant under the trade name TexCare, such as TexCare SRN-170, TexCare SRN-240, TexCare SRN-325. However, these polymers are typically not biodegradable.

[0192] Optical brighteners, particularly for textiles made from cellulose fibers (e.g., cotton), may include derivatives of diaminostilbenedisulfonic acid or its alkali metal salts. Suitable brighteners include salts of 4,4'-bis(2-anilino-4-morpholino-1,3,5-triazin-6-ylamino)stilbene-2,2'-disulfonic acid or similarly structured compounds that carry a diethanolamino group, a methylamino group, or a 2-methoxyethylamino group instead of the morpholino group. Brighteners of the substituted 4,4'-distyryldiphenyl type, e.g., 4,4'-bis(4-chloro-3-sulfostyryl)diphenyl, may also be present. Mixtures of brighteners can also be used. Brighteners of the 1,3-diaryl-2-pyrazoline type, e.g., 1-(p-sulfoamoylphenyl)-3-(p-chlorophenyl)-2-pyrazoline, and similarly structured compounds, are particularly suitable for polyamide fibers. The optical brightener or brightener mixture content of the agent generally does not exceed 1% by weight, preferably 0.05 to 0.5% by weight.-%. In a preferred embodiment of the invention, the agent is free of such active ingredients.

[0193] The conventional foam regulators that can be used in the compositions according to the invention include, for example, polysiloxane-silica mixtures, the finely divided silica contained therein preferably being silanized or otherwise hydrophobized. The polysiloxanes can consist of linear compounds as well as cross-linked polysiloxane resins and mixtures thereof. Other defoamers are paraffin hydrocarbons, in particular microparaffins and paraffin waxes, whose melting point is above 40°C, saturated fatty acids or soaps with, in particular, 20 to 22 C atoms, e.g., sodium behenate, and alkali metal salts of phosphoric acid mono- and / or dialkyl esters, in which the alkyl chains each have 12 to 22 C atoms. Among these, sodium monoalkyl phosphate and / or dialkyl phosphate with C 16-18-alkyl groups are used. The proportion of foam regulators can preferably be 0.2 to 2 wt.%, particularly preferably not more than 1 wt.%.

[0194] To adjust the desired pH, the agents according to the invention can contain system- and environmentally compatible acids, in particular citric acid, acetic acid, tartaric acid, malic acid, lactic acid, glycolic acid, succinic acid, glutaric acid, and / or adipic acid, but also mineral acids, in particular sulfuric acid or alkali metal hydrogen sulfates, or bases, in particular ammonium or alkali metal hydroxides, preferably sodium hydroxide. Such pH regulators are preferably present in the agents according to the invention in amounts of no more than 10% by weight, in particular from 0.5 to 6% by weight, particularly preferably from 0.3 to 2% by weight.

[0195] The agents according to the invention may contain an organic solvent as a further component. The addition of organic solvents has a beneficial effect on the enzyme stability and cleaning performance of these agents. Preferred organic solvents come from the group of mono- or polyhydric alcohols, alkanolamines, or glycol ethers.The solvents are preferably selected from ethanol, n- or i-propanol, butanol, glycol, propanediol, butanediol, glycerin, diglycol, propyl diglycol, butyl diglycol, hexylene glycol, ethylene glycol methyl ether, ethylene glycol ethyl ether, ethylene glycol propyl ether, ethylene glycol mono-n-butyl ether, diethylene glycol methyl ether, diethylene glycol ethyl ether, propylene glycol methyl ether, propylene glycol ethyl ether, propylene glycol propyl ether, dipropylene glycol methyl ether, dipropylene glycol ethyl ether, methoxytriglycol, ethoxytriglycol, butoxytriglycol, 1-butoxyethoxy-2-propanol, 3-methyl-3-methoxybutanol, propylene glycol t-butyl ether and mixtures of these solvents. The weight proportion of these organic solvents in the total weight of the compositions according to the invention is preferably 0.1 to 10 wt.%, preferably 0.2 to 8.0 wt.% and more preferably 0.5 to 5.0 wt.%.A particularly preferred organic solvent that is particularly effective with regard to stabilizing the agents is glycerin and 1,2-propylene glycol. Liquid agents preferably comprise at least one polyol, preferably from the group consisting of glycerin and 1,2-propylene glycol, based on the total weight of the agent, preferably in an amount of 0.1 to 10 wt. %, preferably 0.2 to 8.0 wt. %, and more preferably 0.5 to 5.0 wt. %. Further preferred organic solvents are organic amines and alkanolamines. The agents according to the invention preferably contain these amines in amounts of 0.1 to 10 wt. %, preferably 0.2 to 8.0 wt. % and more preferably 0.5 to 5.0 wt. %, in each case based on their total weight. A particularly preferred alkanolamine is ethanolamine.

[0196] Agents according to the invention can contain enzymes in a concentration appropriate for the effectiveness of the agent. Preferably, all enzymes that can exhibit catalytic activity in the agent according to the invention are used, in particular a protease, lipase, amylase, cellulase, hemicellulase, mannanase, tannase, xylanase, xanthanase, xyloglucanase, β-glucosidase, pectinase, carrageenase, perhydrolase, oxidase, oxidoreductase, and mixtures thereof. Enzymes are advantageously present in the agent in an amount of 1 × 10 -8 to 5 wt.% based on active protein. Increasingly preferably, each enzyme is present in an amount of 1 × 10 -7to 3 wt.%, 0.00001 to 1 wt.%, 0.00005 to 0.5 wt.%, 0.0001 to 0.1 wt.%, and particularly preferably 0.0001 to 0.05 wt.%, based on active protein, in agents according to the invention. Particularly preferably, the enzymes exhibit synergistic cleaning performance against certain soils or stains, i.e., the enzymes contained in the agent composition support each other in their cleaning performance.

[0197] Examples of proteases are subtilisins BPN' from Bacillus amyloliquefaciens and Carlsberg from Bacillus licheniformis, protease PB92, subtilisins 147 and 309, the protease from Bacillus lentus, subtilisin DY, and the enzymes thermitase, proteinase K, and proteases TW3 and TW7, which are classified as subtilases but no longer as subtilisins in the narrower sense. Subtilisin Carlsberg is available in a further developed form under the trade name Alcalase® from Novozymes. Subtilisins 147 and 309 are marketed by Novozymes under the trade names Esperase® and Savinase®, respectively. Protease variants are derived from the protease from Bacillus lentus DSM 5483, described in e.g. WO 95 / 23221, WO 92 / 21760 WO 2013 / 060621 and EP 3660151. Other useful proteases are e.g.the enzymes available under the trade names Durazym®, Relase®, Everlase®, Nafizym®, Natalase®, Kannase®, Progress Uno 101L® and Ovozyme® from Novozymes, the enzymes available under the trade names Purafect®, Purafect® OxP, Purafect® Prime, Excellase®, Properase®, Preferenz P100® and Preferenz P300® from Danisco / DuPont, the enzyme available under the trade name Lavergy pro 104 LS® from BASF, the enzyme available under the trade name Protosol® from Advanced Biochemicals Ltd., the enzyme available under the trade name Wuxi® from Wuxi Snyder Bioproducts Ltd., the enzyme available under the trade names Proleather® and Protease P® from Amano Pharmaceuticals Ltd., and the enzyme available under the name Proteinase K-16 from Kao Corp. The proteases from Bacillus gibsonii and Bacillus pumilus, which are disclosed in WO 2008 / 086916, WO 2007 / 131656, WO 2017 / 215925, WO 2021 / 175696 and WO 2021 / 175697, are also particularly preferably used.

[0198] Examples of amylases include the α-amylases from Bacillus licheniformis, Bacillus amyloliquefaciens, or Bacillus stearothermophilus, as well as their improved versions for use in detergents and / or cleaning agents. The enzyme from Bacillus licheniformis is available from Novozymes under the name Termamyl® and from Danisco / DuPont under the name Purastar® ST. Further developments of this α-amylase are available under the trade names Duramyl® and Termamyl® ultra (both from Novozymes), Purastar® OxAm (Danisco / DuPont), and Keistase® (Daiwa Seiko Inc.). The α-amylase from Bacillus amyloliquefaciens is marketed by Novozymes under the name BAN®, and derivatives of the α-amylase from Bacillus stearothermophilus are marketed under the names BSG® and Novamyl®, also by Novozymes. Furthermore, the α-amylase from Bacillus sp. is available for this purpose.A 7-7 (DSM 12368) and cyclodextrin glucanotransferase (CGTase) from Bacillus agaradherens (DSM 9948) are particularly suitable. Fusion products of all of the above-mentioned molecules can also be used. Furthermore, the further developments of α-amylase from Aspergillus niger and A. oryzae, available under the trade name Fungamyl® from Novozymes, are also suitable. Other commercial products that can be used advantageously include Amylase-LT® and Stainzyme® or Stainzyme® ultra or Stainzyme® plus, as well as Amplify™ 12L or Amplify Prime™ 100L, the latter also from Novozymes, and the PREFERENZ S® series from Danisco / DuPont, including PREFERENZ S100®, PREFERENZ S1000®, and PREFERENZ S210®. Variants of these enzymes obtainable by point mutations can also be used according to the invention.

[0199] Suitable cellulases include those of bacterial or fungal origin. Chemically modified or protein-engineered mutants are also included. Suitable cellulases are cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, and Acremonium, e.g., the fungal cellulases from Humicola insolens, Myceliophthora thermophila, and Fusarium oxysporum, disclosed in US 4,435,307, US 5,648,263, US 5,691,178, US 5,776,757, and WO 89 / 09259. Particularly suitable cellulases are alkaline or neutral cellulases with color-care properties. Examples of such cellulases are cellulases described in EP 0495257, EP 0531372, WO 96 / 11262, WO 96 / 29397, WO 98 / 08940. Other examples are cellulase variants as described in WO 94 / 07998, EP 0531315, EP 3212777, EP 3502243, EP 3653705, EP 3653706, US 5457046, US 5686593, US 5763254, WO 95 / 24471, WO 98 / 12307, WO 99 / 01544, and WO 2019 / 122520.Examples of cellulases with endo-1,4-glucanase activity (EC 3.2.1.4) are described in WO 2002 / 099091, e.g., those having a sequence of at least 97% identity to the amino acid sequence of positions 1 to 773 of SEQ ID NO:2 of WO 2002 / 099091. Another example may comprise a GH44 xyloglucanase, e.g., a xyloglucanase enzyme having a sequence of at least 60% identity to positions 40 to 559 of SEQ ID NO:2 of WO 2001 / 062903. Other examples of cellulases include the GH45 cellulases described in WO 96 / 29397. Commercially available cellulases include Celluzyme™, Carezyme™, Carezyme Premium™, Celluclean™ (e.g. Celluclean™ 5000L and Cellulclean™ 4000T), Celluclean Classic™, Cellusoft™, Endolase®, Renozyme® and Whitezyme™ (Novozymes A / S), Clazinase™ and Puradax HA™ (Genencor International Inc.), KAC-500(B)™ (Kao Corporation), Revitalenz™ 1000, Revitalenz™ 2000 and Revitalenz™ 3000 (DuPont), as well as Ecostone® and Biotouch® (AB Enzymes).

[0200] Suitable lipases are, for example, from Thermomyces, e.g. from T. lanuginosus (formerly Humicola lanuginosa), as described in EP 0258068 and EP 0305216, lipase from strains of Pseudomonas (some of them now renamed Burkholderia), e.g. P. alcaligenes or P. pseudoalcaligenes, P. cepacia, P. sp. strain SD705, P. wisconsinensis, Streptomyces lipases of the GDSL type, lipase from Thermobifida fusca, lipase from Geobacillus stearothermophilus, lipase from Bacillus subtilis and lipase from Streptomyces griseus and S. pristinaespiralis. Preferred lipases include, for example, the lipases originally obtainable from Humicola lanuginosa (Thermomyces lanuginosus) or further developed therefrom, in particular those with one or more of the following amino acid substitutions starting from the said lipase in the positions D96L, T213R and / or N233R, particularly preferably T213R and N233R.Preferred commercial lipase products include Lipolase™, Lipex™, Lipolex™ and Lipoclean™ (Novozymes A / S), Lumafast (Genencor / DuPont) and Lipomax (Gist-Brocades).

[0201] Suitable mannanases are, for example, the Bacillus subtilis endo-β-mannanase, Bacillus sp. I633 Endo-β-mannanase, Bacillus sp. AAI12 endo-β-mannanase, Bacillus sp. AA349 Endo-β-mannanase, Bacillus agaradhaerens NCIMB 40482 Endo-β-mannanase, Bacillus halodurans Endo-β-mannanase, Bacillus clausii Endo-β-mannanase, Bacillus licheniformis Endo-β-mannanase, Humicola insolens Endo-β-mannanase and Caldocellulosiruptor sp. Endo-β-mannanase (see e.g. US 6060299, WO 99 / 64573, US 6566114 and WO 99 / 64619).

[0202] Pectate lyases suitable for detergents and cleaning agents are described, for example, in WO 2003 / 095638 or WO 2015 / 121133. Examples of suitable pectinolytic enzymes include the enzymes and enzyme preparations available under the trade names Gamanase®, Pektinex AR®, X-Pect®, or Pectaway® from Novozymes, under the trade names Rohapect UF®, Rohapect TPL®, Rohapect PTE100®, Rohapect MPE®, Rohapect MA plus HC, Rohapect DA12L®, Rohapect 10L®, Rohapect B1L® from AB Enzymes, and under the trade name Pyrolase® from Diversa Corp.

[0203] In the cleaning agents described herein, the enzymes to be used can also be formulated together with accompanying substances, such as those from fermentation. In liquid formulations, the enzymes are preferably used as liquid enzyme formulation(s).

[0204] Furthermore, it is possible to package two or more enzymes together so that a single granulate has multiple enzyme activities.

[0205] The enzymes can also be incorporated into water-soluble films, such as those used, for example, in the packaging of unit-dose detergents and cleaning agents. Such a film allows the enzymes to be released upon contact with water. As used herein, "water-soluble" refers to a film structure that is preferably completely water-soluble. Preferably, such a film consists of (fully or partially hydrolyzed) polyvinyl alcohol (PVA).

[0206] The agents according to the invention can comprise one or more reversible enzyme inhibitors / stabilizers. The agents according to the invention can contain the reversible enzyme inhibitors / stabilizers in a concentration of 0.1 to 2 wt.%, preferably 0.3 to 1.5 wt.%, based on the total weight of the agent. If multiple inhibitors / stabilizers are present, these values ​​refer to the total concentration. These can be selected, in particular, from the group consisting of polyols such as glycerol or 1,2-ethylene glycol, benzamidine hydrochloride, borax, boric acids, boronic acids or their salts or esters or derivatives, in particular phenylboronic acid derivatives or 4-formylphenylboronic acid (4-FPBA), antioxidants, special peptide compounds, and combinations thereof.

[0207] In particularly preferred embodiments, the washing and / or cleaning agent according to the invention is substantially free of boron-containing compounds. "Substantially free of boron-containing compounds" in this context means that the agents according to the invention contain less than 2% by weight, preferably less than 1% by weight, more preferably less than 0.5% by weight, and particularly preferably less than 0.1% by weight, of boron-containing compounds, based on the total weight of the agent. In very particularly preferred embodiments, the agents according to the invention are free of boron-containing compounds, i.e., they contain in particular no boric acid and / or phenylboronic acid derivatives.

[0208] Further suitable additives for agents according to the invention can be selected from, for example, builders, bleaching agents, bleach catalysts, bleach activators, electrolytes, pH adjusters, perfumes, perfume carriers, fluorescent agents, dyes, dye transfer inhibitors (DTI polymers), hydrotropes, foam inhibitors / defoamers, silicone oils, soil release polymers / soil repellent polymers, graying inhibitors, shrinkage inhibitors, crease inhibitors, antimicrobial agents, solvents, germicides, fungicides, antioxidants, preservatives, corrosion inhibitors, antistatic agents, bittering agents, ironing aids, repellents and impregnating agents, skin-care agents, swelling and slip-resistant agents, complexing agents, softening components as well as UV absorbers and mixtures thereof, in particular solvents such as water and / or organic solvents, thickeners, stabilizers, Soil-release polymers / soil-repellent polymers, fragrances or perfumes,Complexing agents, pH adjusters, foam inhibitors / defoamers and / or mixtures thereof.

[0209] In a preferred embodiment, the agent according to the invention comprises the at least one additive in an amount of 0.0001 to 30 wt.%, preferably 0.1 to 20 wt.%, more preferably 1 to 10 wt.%, based on the total weight of the agent. Water is preferably not included in this concentration and can be added to the agent in addition.

[0210] The product preferably contains at least one perfume or fragrance, or optionally a mixture of different perfumes or fragrances as the at least one additive. Individual fragrance compounds, e.g. synthetic products of the ester, ether, aldehyde, ketone, alcohol and hydrocarbon type, can be used as perfume oils or fragrances. However, mixtures of different fragrances are preferably used which together create an appealing fragrance. Such perfume oils can also contain natural fragrance mixtures, such as those obtainable from plant sources, e.g. pine, citrus, jasmine, patchouli, rose or ylang-ylang oil. Suitable fragrances and perfumes or mixtures thereof are known to those skilled in the art in the field of detergent or cleaning product production. In a preferred embodiment, the product contains one or more fragrances in an amount of usually up to 15% by weight, preferably 0.01 to 5% by weight.-%, in particular 0.3 to 3 wt.%, based on the total weight of the agent.

[0211] In a preferred embodiment of the invention, the agents contain one or more hydrophobic components. The hydrophobic components not only improve the cleaning effect against hydrophobic contaminants such as greasy soils, but also have a positive effect on phase separation and its reversibility in multiphase agents. Suitable hydrophobic components are, for example, dialkyl ethers with the same or different C 4-14-Alkyl radicals, in particular linear dioctyl ether; hydrocarbons with a boiling range of 100 to 300°C, in particular 140 to 280°C, e.g. aliphatic hydrocarbons with a boiling range of 145 to 200°C, isoparaffins with a boiling range of 200 to 260°C; essential oils, in particular limonene and pine oil extracted from pine roots and stumps; and also mixtures of these hydrophobic components, in particular mixtures of two or three of the hydrophobic components mentioned. Preferred mixtures of hydrophobic components are mixtures of various dialkyl ethers, of dialkyl ethers and hydrocarbons, of dialkyl ethers and essential oils, of hydrocarbons and essential oils, of dialkyl ethers and hydrocarbons and essential oils, and of these mixtures. The washing or cleaning agents may contain hydrophobic components in amounts, based on the total weight of the agent, of 0.01 to 20 wt.%, preferably 0.1 to 14 wt.-%, more preferably 0.5 to 10 wt.%, even more preferably 0.8 to 7 wt.%.

[0212] If the washing or cleaning agents according to the invention are formulated in multiple phases, they can contain one or more phase separation aids. Suitable phase separation aids, in addition to citric acid or citrates, include, for example, alkali metal and alkaline earth metal halides, in particular chlorides, and sulfates and nitrates, in particular sodium and potassium chloride and sulfate, as well as ammonium chloride and sulfate, or mixtures thereof. Such salts, as strong electrolytes which increase ionic strength, support phase separation through the salt effect. Sodium chloride has proven particularly effective in this regard, while sodium sulfate and in particular magnesium sulfate have less of a phase-separating effect. The washing or cleaning agents can contain phase separation aids in amounts, based on the total weight of the agent, of 0.01 to 30% by weight, preferably 0.1 to 20% by weight, e.g. 1 to 15% by weight or 1 to 5% by weight.

[0213] To adjust the viscosity, the washing or cleaning agent may contain one or more thickeners, preferably in an amount of 0.01 to 5% by weight, more preferably 0.05 to 2.5% by weight, even more preferably 0.1 to 1% by weight. Suitable thickeners are, for example, organic natural thickeners (agar-agar, carrageenan, tragacanth, gum arabic, alginates, pectins, polyoses, guar flour, locust bean gum, starch, dextrins, gelatin, casein), organic modified natural substances (carboxymethylcellulose and other cellulose ethers, hydroxyethyl and propylcellulose and the like, kernel flour ethers), organic fully synthetic thickeners (polyacrylic and polymethacrylic compounds, vinyl polymers, polycarboxylic acids, polyethers, polyimines, polyamides) and inorganic thickeners (polysilicic acids, clay minerals such as montmorillonites, zeolites, silicas).

[0214] Polyacrylic and polymethacrylic compounds include, for example, the high-molecular-weight homopolymers of acrylic acid crosslinked with a polyalkenyl polyether, in particular an allyl ether of pentaerythritol or propylene (INCI name according to the International Dictionary of Cosmetic Ingredients of the Cosmetic, Toiletry, and Fragrance Association (CTFA): carbomer), which are also referred to as carboxyvinyl polymers. Furthermore, the following acrylic acid copolymers fall under this category: (i) Copolymers of two or more monomers from the group of acrylic acid, methacrylic acid and their simple, preferably C 1-4 -alkanols, esters (INCI Acrylates Copolymer), which include the copolymers of methacrylic acid, butyl acrylate and methyl methacrylate (CAS 25035-69-2) or of butyl acrylate and methyl methacrylate (CAS 25852-37-3); (ii) cross-linked high molecular weight acrylic acid copolymers, which include the copolymers of C cross-linked with an allyl ether of pentaerythritol 10-30-alkyl acrylates with one or more monomers from the group of acrylic acid, methacrylic acid and their simple, preferably C 1-4 -alkanols formed, esters (INCI Acrylates / C 10-30 Alkyl Acrylate Crosspolymer). In addition to the thickening effect, these compounds can have other effects in detergents, such as anti-graying properties. In a preferred embodiment, the polyacrylic and polymethacrylic compounds suitable as thickeners have a weight-average molecular weight of >100,000 g / mol, preferably <500,000 g / mol.

[0215] Preferred thickeners are polysaccharides and heteropolysaccharides, especially polysaccharide gums, e.g., gum arabic, agar, alginates, carrageenans and their salts, guar, guaran, tragacanth, gellan, ramsan, dextran, or xanthan gum and their derivatives, e.g., propoxylated guar, and mixtures thereof. Other polysaccharide thickeners, such as starches or cellulose derivatives, can be used alternatively, but preferably in addition, to a polysaccharide gum, e.g., starches of various origins and starch derivatives, e.g., hydroxyethyl starch, starch phosphate esters, or starch acetates, or carboxymethylcellulose or its sodium salt, methyl, ethyl, hydroxyethyl, hydroxypropyl, hydroxypropylmethyl, or hydroxyethylmethylcellulose, or cellulose acetate. Polysaccharides and heteropolysaccharides suitable as thickeners preferably have a weight-average molecular weight of >1500 g / mol, more preferably >5000 g / mol, even more preferably >50000 g / mol.Generally, their weight-average molecular weight is <250,000 g / mol. A particularly preferred polymer is the microbial anionic heteropolysaccharide xanthan gum, which is produced by Xanthomonas campestris and some other species under aerobic conditions with a molecular weight of 2 to 15 × 10. 6 g / mol is produced.

[0216] In various embodiments, the washing or cleaning agent according to the invention can contain dye transfer inhibitors, preferably DTI (dye transfer inhibiting) polymers. Suitable DTI polymers include, for example, homo- or copolymers based on vinylic, nitrogen-containing, preferably heterocyclic monomers, e.g., N-vinylpyrrolidone, N-vinylimidazole, N-vinylcaprolactam, and 4-vinylpyridine. These compounds are typically not biodegradable. Examples of commercially available DTIs are known from US 2012 / 0225025 A1. Other examples of DTI polymers include, but are not limited to, polyvinylpyrrolidone (e.g., Sokalan® HP 50 / BASF, PVP-K-Typen® / ISP), vinylpyrrolidone-vinylimidazole copolymers (e.g., Sokalan® HP 56 / BASF), poly(4-vinylpyridine-N-oxide) (e.g., Chromabond® S-403E / ISP), and poly(4-vinylpyridine-N-carboxymethylbetaine) (e.g., Chromabond® S 400 / ISP).

[0217] Exemplary washing and cleaning agent compositions and suitable ingredients are described, for example, in WO 2001 / 44433 A1 or WO 2016 / 091650 A1.

[0218] An exemplary composition of a detergent according to the invention, in particular a liquid detergent, comprises, in addition to the peptides and / or peptide conjugates described herein, the following components: water; and surfactants, in particular anionic and / or non-ionic surfactants; and / or thickeners; and / or stabilizers; and / or organic solvents; and / or enzymes; and / or fragrances; and / or complexing agents, e.g. phosphonates, in particular HEDP; and / or pH adjusters, in particular citric acid, NaOH and / or monoethanolamine (MEA); and / or dye transfer inhibitors, in particular DTI polymers; and / or optionally further soil release polymers / soil repellent polymers; and / or antifoams.

[0219] A washing or cleaning agent according to the invention particularly preferably comprises, in addition to the peptides according to the invention, the following components: at least one surfactant, preferably in a concentration of 0.5 to 60 wt.%; and / or at least one stabilizer, preferably in a concentration of 0.001 to 20 wt.%, e.g. 0.1 to 5 wt.%; and / or at least one complexing agent, preferably in a concentration of 0.01 to 30 wt.%, in particular 0.1 to 10 wt.% or 0.2 to 5 wt.%; and / or at least one organic solvent, preferably in a concentration of 0.1 to 30 wt.%, e.g. 0.5 to 25 wt.%; and / or at least one DTI polymer, preferably in a concentration of 0.01 to 20 wt.%, for example 0.05 to 5 wt.%; and / or at least one enzyme, preferably in a concentration of 0.00001 to 5 wt.%; and / or at least one fragrance or perfume substance and / or at least one fragrance storage substance, preferably in a concentration of 0.0001 to 15 wt.-%; and / or at least one pH adjuster, e.g. MEA, NaOH or citric acid, preferably in a concentration of 0.01 to 25 wt.%, e.g. 0.05 to 20 wt.%; and / or at least one antifoam, preferably in a concentration below 5 wt.%, e.g. below 2 wt.% such as below 1 wt.%; and / or water; in each case based on the total weight of the washing or cleaning agent. Washing or cleaning performance

[0220] For the purposes of the invention, cleaning performance refers to the ability of a product to partially or completely remove existing soiling, in particular the brightening performance of one or more types of soiling on textiles. Cleaning performance is preferably determined as specified below.

[0221] Wash liquor refers to the working solution containing the detergent that acts on the textiles or fabrics and thus comes into contact with the soiling present on them. The wash liquor is typically created when the washing process begins and the detergent is diluted with water, for example, in a washing machine or another suitable container.

[0222] The cleaning performance can be determined in a washing system containing a detergent at a dosage between 2.0 and 8.0 grams per liter of wash liquor and the peptides to be investigated.

[0223] A liquid reference detergent for such a washing system can, for example, be composed as follows (all data in weight percent (wt%)): 4.4% alkylbenzenesulfonic acid, 5.6% other anionic surfactants, 2.4% C 12-18Na salts of fatty acids (soaps), 4.4% non-ionic surfactants, 0.2% phosphonates, 1.4% citric acid, 0.95% NaOH, 0.01% defoamer, 2% glycerin, 0.08% preservatives, 1% ethanol, balance demineralized water. The dosage of the liquid detergent is preferably between 3.0 and 6.0 grams per liter of wash liquor, for example 3.0, 3.2, 3.5, 3.7, 4.0, 4.5, 4.7, 4.9, or 5.9 grams per liter of wash liquor. Washing is preferably carried out in a pH range between pH 7 and pH 10.5, preferably between pH 8 and pH 9.

[0224] The cleaning performance of a textile is determined by measuring the degree of cleanliness of the washed textiles. For example, the wash cycle can be carried out for 60 minutes at a temperature of 40°C and the water hardness can be between 15.5°dH and 16.5°dH (German hardness).

[0225] The degree of whiteness, i.e., the lightening of soils, as a measure of cleaning performance, is determined using optical measurement methods, preferably photometrically. A suitable device for this purpose is the Minolta CM508d spectrometer. The devices used for the measurement are usually calibrated beforehand with a white standard, preferably one supplied with the product.

[0226] Preferred embodiments of agents according to the invention achieve such advantageous cleaning performance even at low temperatures, in particular in the temperature ranges between 10°C and 60°C, preferably between 15°C and 50°C and particularly preferably between 20°C and 40°C. Processes and uses

[0227] A further subject matter of the invention is a method for cleaning textiles and / or hard surfaces, in particular dishes, which is characterized in that an agent according to the invention is used in at least one method step.

[0228] In various embodiments, the process described above is characterized in that it is carried out at a temperature of 0°C to about 100°C, preferably about 20°C to about 60°C, particularly preferably about 20°C to about 40°C. 20°C represents low wash temperature, while 40°C is the preferred / average wash temperature in Europe.

[0229] This includes both manual and mechanical processes, with mechanical processes being preferred due to their more precise controllability, for example, regarding the quantities used and contact times. Processes for cleaning textiles are generally characterized by the application of various cleaning agents to the items to be cleaned in several steps and their subsequent washing off after the contact time, or by the items to be cleaned being treated in some other way with a detergent or a solution or dilution of this agent.

[0230] The method preferably relates to a machine washing process, in particular in a washing machine, or a hand washing process. The peptide and / or peptide conjugate described herein preferably acts as a soil-repellent and / or soil-removing agent.

[0231] This subject matter of the invention also encompasses a machine dishwashing process. In such a process, the agent according to the invention can be dosed into the cleaning solution, for example, by means of the dosing chamber in the door or by means of an additional dosing container in the interior of the dishwasher. Alternatively, the agent can also be applied directly to the soiled dishes or to one of the interior walls of the dishwasher, for example the inside of the door. The process according to the invention is carried out in the interior of a commercially available dishwasher. In a dishwasher, the cleaning program can generally be selected and set by the consumer before the dishwashing process is carried out. The cleaning program of the dishwasher used in the process according to the invention comprises at least one pre-wash cycle and one cleaning cycle.According to the invention, cleaning programs are preferred which comprise further cleaning or rinsing cycles, e.g. a final rinse cycle. The method according to the invention is particularly preferably a component of a cleaning program comprising a pre-rinse cycle, a cleaning cycle and a final rinse cycle. The method according to the invention is preferably used in conjunction with cleaning programs in which the wash liquor is heated during the cleaning cycle. In a preferred embodiment of the method according to the invention, the cleaning cycle, during which the agent according to the invention is metered into the interior of the dishwasher, is characterized in that during its course the temperature of the cleaning liquor rises to values ​​above 30°C, preferably above 40°C and in particular above 50°C.

[0232] Alternative embodiments of this subject matter of the invention also include processes for treating textile raw materials or for textile care, in which an agent according to the invention is active in at least one process step. Among these, processes for textile raw materials, fibers, or textiles with natural components are preferred, and especially for those containing wool or silk.

[0233] A further subject matter of the invention is the use of an agent according to the invention for cleaning textiles and / or hard surfaces, in particular dishes, preferably in a temperature range of about 20°C to about 60°C, particularly preferably about 20°C to about 40°C.

[0234] A further subject matter of the invention is the use of a peptide and / or peptide conjugate described herein in a washing or cleaning agent according to the invention for improving the cleaning performance of the washing or cleaning agent on grease and / or oil-containing soils, preferably in a temperature range of about 20°C to about 60°C, particularly preferably about 20°C to about 40°C.

[0235] A further subject of the invention is the use of a peptide as a soil-removing and / or soil-repellent active ingredient in a washing or cleaning agent, preferably a textile detergent, wherein the peptide is selected from (A) a peptide with the following amino acid sequence: (C)mX1X2X3(X4)nX5(C)o, where X1 is a positively charged amino acid, preferably R or K, more preferably R, X2 and X3 are uncharged amino acids, preferably A, L, S, I, M or Q, more preferably A, S, I or L, particularly preferably A or L, each X4 independently of one another is any amino acid, preferably with the exception of P, more preferably with the exception of P and G, X5 is any positively charged or uncharged amino acid, preferably R or an uncharged amino acid, more preferably Q, A or L, particularly preferably A or L, m and o are 0 or 1, where m+o = 0 or 1, and n is an integer from 0 to 46, preferably 6 to 20, more preferably 6 to 12, particularly preferably 8 to 12, wherein the peptide is preferably a textile-binding peptide; and / or (B) a peptide having an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences mentioned in SEQ ID NO:1-27, wherein the peptide is preferably a textile-binding peptide.

[0236] A further subject of the invention is the use of a peptide conjugate as a soil-removing and / or soil-repellent active ingredient in a washing or cleaning agent, preferably a textile detergent, wherein the peptide conjugate has the following sequence in N- to C-terminal orientation: (Z1)p(Z2)q(Z3)r(Z4)s(Z5)t(Z6)v(Z7)w, wherein Z4 is a peptide, preferably a textile-binding peptide, selected from (A) a peptide with the following amino acid sequence: (C)mX1X2X3(X4)nX5(C)o, where C is the amino acid cysteine, where m+o = 0 or 1; where X1 is a positively charged amino acid, preferably R or K, more preferably R, X2 and X3 are uncharged amino acids, preferably A, L, S, I, M or Q, more preferably A, S, I or L, particularly preferably A or L, each X4 independently of one another is any amino acid, preferably with the exception of P, more preferably with the exception of P and G, X5 is any positively charged or uncharged amino acid, preferably R or an uncharged amino acid, more preferably Q, A or L, particularly preferably A or L, m and o are 0 or 1, where n is an integer from 0 to 46, preferably 6 to 20, more preferably 6 to 12, particularly preferably 8 to 12, (B) a peptide having an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NO: 1-27, where s = 1; where Z1 and Z7 are independently -(C2H4O) k where k = 5-100, preferably k = 20-85, preferably k = 30-75, particularly preferably k = 40-60, very particularly preferably k = 45, p and w are 0 or 1 and p+w = 0 to 2; wherein Z2 and Z6 are independently a peptide, preferably a textile-non-binding peptide, which has an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with the amino acid sequence given in SEQ ID NO:28, wherein q and v are 0 or 1 and q+v = 0 to 2; wherein Z3 and Z5 are linkers, preferably peptide linkers, wherein r and t are 0 or 1 and r+t = 0 to 2; where p+q+r+t+v+w = 2 to 6, preferably 3 to 5, particularly preferably 3 or 4, most preferably.

[0237] In preferred embodiments, the use of the peptide and / or peptide conjugate leads to a soil-removing and / or soil-repellent effect, i.e., the peptide and / or peptide conjugate effects a soil-removing and / or soil-repellent effect on textiles, preferably during the washing or cleaning process, more preferably as a component of a washing or cleaning agent. In particular, the textiles are freed from soil and / or protected from renewed soil deposition by the presence of the peptide and / or peptide conjugate, which preferably binds and / or adheres to textiles, preferably plastic-containing textiles, preferably polyester-containing textiles, or blended fabrics.Due to the adhering peptides and / or peptide conjugates, the dirt-repellent effect of the peptides and / or peptide conjugates is particularly realized after several wash cycles, since the dirt is less likely to deposit on or between the fibers due to the adhering peptides and / or peptide conjugates.

[0238] All facts, objects, and embodiments described for the agent according to the invention are also applicable to these subject matters of the invention. Therefore, express reference is made here to the disclosure at the appropriate point, with the note that this disclosure also applies to the above-mentioned use according to the invention. EXAMPLESExample 1: Peptide sequences

[0239] The peptides shown in Table 1 were prepared by chemical synthesis. Table 1: Peptide sequences peptide Amino acid sequence SEQ ID NO 1 (PEG)-GGGGS-RSIVTFSLRQNR-GGGGS-(PEG) 41 2 (PEG)-GGGGS-RALQALRALQALEAL-GGGGS-(PEG) 42 3 (PEG)-GGGGS-RALRALQALEEALEAL-GGGGS-(PEG) 43 4 NGLLIPQFLVAS-GGGGS-RSIVTFSLRQNR-GGGGS-NGLLIPQFLVAS 44 5 NGLLIPQFLVAS-GGGGS-RALQALRALQALEAL-GGGGS-NGLLIPQFLVAS 45 6 NGLLIPQFLVAS-GGGGS-RALRALQALEEALEAL-GGGGS-NGLLIPQFLVAS 46 7 RSIVTFSLRQNR 25 8 RALQALRALQALEAL 1 9 RALRALQALEALEAL 5 10 NGLLIPQFLVAS 28 11 GGGGS 29

[0240] In Table 1, (PEG) means that the respective amino acid sequence has a polyethylene glycol (PEG; 45 units; 2 kDa) at the N- and / or C-terminus.

[0241] Peptides 1 to 6 are peptide conjugates comprising (i) a PEG chain or a textile-nonbinding peptide (peptide 10), (ii) a first peptide linker (peptide 11), (iii) a textile-binding peptide (one of peptides 7 to 9), (iv) a second peptide linker (peptide 11), and (v) a PEG chain or a textile-nonbinding peptide (peptide 10).

[0242] Peptides 7 to 9 are textile-binding peptides.

[0243] Peptide 10 is a textile-nonbinding peptide.

[0244] Peptide 11 is a peptide linker. Example 2: Adhesion test of peptides on polyester and blended fabrics

[0245] The adhesion of peptides 7 to 10 according to Table 1 to polyester fabric (WFK 30A, 100% polyester) and cotton / polyester blend fabric (WFK 20A, 50% cotton / 50% polyester) was tested.

[0246] Test setup: Measurement method with fluorescamine in 48-well microtiter plate with cloth pads with a diameter of 10 mm.

[0247] Three lobules per peptide dilution were placed in the 48-well microtiter plate, and 0.2 ml of peptide solution (0.02 mg / ml in distilled water) was added to each. The plate was incubated for 1 h at RT, shaking at 750 rpm. Subsequently, 50 µl of the supernatant was transferred to a black 96-well microtiter plate, and fluorescamine solution (final concentration 1 mg / ml) was added, mixed, and incubated at RT for 16 min. Fluorescence was measured immediately afterwards (absorbance 340 nm, emission 465 nm).

[0248] Fluorescamine binds to the free primary amino group of a peptide. The more peptides bound to the textile patches, the fewer peptides with free amino groups are present in the supernatant. Since fluorescamine exhibits no fluorescence without derivatization, the more fluorescamine-peptide conjugates present in the supernatant, the higher the fluorescence. The measured fluorescence values ​​were converted to % adhesion as follows: (BA) / A, where B is the measured value for the test sample and A is the measured value for the blank.

[0249] Table 2 shows the percentage of the applied peptide (100%) that adheres to the respective textile. The higher the value, the higher the binding affinity. Table 2: Adhesion of peptides to test tissue Peptide 7 Peptide 8 Peptide 9 Peptide 10 WFK 20A 97,4% 90,2% 80,7% 0% WFK 30A 89,5% 85,3% 90,7% 0%

[0250] Peptides 7 to 9 show a high binding affinity and are therefore textile-binding peptides.

[0251] Peptide 10 shows no binding affinity, thus it is a textile-nonbinding peptide. Example 3: Washing test

[0252] A conventional soil release polymer (poly[terephthalic acid-co-propylene glycol-co-PEG750 monomethyl ether]; 0.25% active ingredient) (comparative example) or a peptide according to the invention (peptides 1 to 6; 2% by weight of active ingredient in the formulation) was incorporated into a detergent matrix according to Table 3. Table 3: Detergent matrix Chemical name % wt. active substance in raw material % wt. active substance in the formulation demineralized water 100 to 100 Defoamers 100 <1% citric acid 100 1-5% FAEOS 70 3-8% FAEO 100 2-11% LAS 96 3-20% C 12 -C 18 fatty acid sodium salt 30 0,3-4% Monoethanolamine 100 4-8% NaOH 50 0,5-2% Glycerin 99,5 1-3% 1,2-Propanediol 100 8-12% Phosphonate (HEDP) 60 0,5-2% Perfumes, enzymes tq Minors stabilizer 100 0-1% Dosage 3.1 g / l; pH 8.2-8.4 Table 4: Experimental approaches A B C D E F G Soil Release Polymer 0,25% 0% 0% 0% 0% 0% 0% Peptide 1 0% 2% 0% 0% 0% 0% 0% Peptide 2 0% 0% 2% 0% 0% 0% 0% Peptide 3 0% 0% 0% 2% 0% 0% 0% Peptide 4 0% 0% 0% 0% 2% 0% 0% Peptide 5 0% 0% 0% 0% 0% 2% 0% Peptide 6 0% 0% 0% 0% 0% 0% 2% Table 5: Washing conditions Device Linitest Plus, Atlas Washing temperature 40°C Water hardness 16°dH Washing time 30 minutes dosage 3,1 g / l Washing volume 200 ml rotation 40 rpm tissue WFK 30A, WFK 20A Soiling 25 µl engine oil Repetitions 3

[0253] The textile fabrics were pre-washed, rinsed, and dried three times using the respective detergent formulation to be tested. 25 µl of engine oil was applied to each of the pre-washed textile fabrics and dried. The soiled textile fabrics were then washed with the respective detergent formulation to be tested, rinsed, and dried. The brightening of the soils was measured using a Spectraflash SF600. The measured values ​​are presented in Table 6 as the Y-value (whiteness). The higher the value, the better the brightening performance. A difference of ≥ 0.5 is considered significant. Table 6: Whitening performance A B C D E F G WFK 20A 59,8 59,8 60,3 58,4 62,6 61,5 60,2 WFK 30A 59,2 57,1 58,5 58,7 59,1 60,2 60,3

[0254] The peptides according to the invention lead to a whitening performance comparable to the reference sample (A) (peptides 1, 3) or even better (peptides 2, 4, 5, 6). Peptides 4 and 5, in particular, demonstrate improved whitening performance on mixed fabrics. The improved whitening performance demonstrates that the peptides not only contribute to cleaning performance but also indicate a soil-repellent and / or soil-removing effect. QUOTES CONTAINED IN THE DESCRIPTION

[0000] This list of documents submitted by the applicant was generated automatically and is included solely for the convenience of the reader. This list is not part of the German patent or utility model application. The DPMA assumes no liability for any errors or omissions. Cited patent literature

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[0217]

Claims

[1] Washing or cleaning agents, preferably textile washing agents, comprising at least one peptide and / or peptide conjugate, wherein the at least one peptide and / or peptide conjugate has the following sequence in N- to C-terminal orientation: (Z1)p(Z2)q(Z3)r(Z4)s(Z5)t(Z6)v(Z7)w, wherein Z4 is a peptide, preferably a textile-binding peptide, selected from (A) a peptide with the following amino acid sequence: (C)mX1X2X3(X4)nX5(C)o, where C is the amino acid cysteine, where m+o = 0 or 1; where X1 is a positively charged amino acid, preferably R or K, more preferably R, X2 and X3 are uncharged amino acids, preferably A, L, S, I, M or Q, more preferably A, S, I or L, particularly preferably A or L, each X4 independently of one another is any amino acid, preferably with the exception of P, more preferably with the exception of P and G, X5 is any positively charged or uncharged amino acid, preferably R or an uncharged amino acid, more preferably Q, A or L, particularly preferably A or L, m and o are 0 or 1, where n is an integer from 0 to 46, preferably 6 to 20, more preferably 6 to 12, particularly preferably 8 to 12, (B) a peptide having an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NO: 1-27, where s = 1; where Z1 and Z7 are independently -(C2H4O) k where k = 5-100, p and w are 0 or 1 and p+w = 0 to 2; wherein Z2 and Z6 are independently a peptide, preferably a textile-non-binding peptide, which has an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with the amino acid sequence given in SEQ ID NO:28, wherein q and v are 0 or 1 and q+v = 0 to 2; wherein Z3 and Z5 are linkers, preferably peptide linkers, wherein r and t are 0 or 1 and r+t = 0 to 2; where p+q+r+t+v+w = 0 to 6, preferably 3 to 5, particularly preferably 3 or 4, most preferably 4. [2] Washing or cleaning agent according to claim 1, wherein (i) the peptide (A) has a total charge of 0 to +4, preferably 0 to +2, and / or (ii) the N-terminus of the peptide (A) comprising the first 3-4 amino acids has a positive net charge, and / or (iii) the C-terminus of the peptide (A) comprising the last 3-6 amino acids has a negative or neutral net charge and preferably comprises at least one negatively charged amino acid, in particular E, and / or (iv) the peptide (A) does not contain P and preferably also does not contain G and more preferably also does not contain Y. [3] Washing or cleaning agent according to claim 1 or 2, wherein (i) the sequence X1X2X3 is RSI, RAL or RLA, preferably RSI or RAL; and / or (ii) (X4) n X5 comprises at least one sequence X6X7X8, where X6 is a charged or uncharged amino acid, preferably R, K, E or Q, and X7 and X8 are independently uncharged amino acids with the exception of P and G, preferably A, L, or M, more preferably A or L, and / or (iii) (X4) n at least one aromatic amino acid, preferably W or F. [4] Washing or cleaning agent according to one of the preceding claims, wherein (i) (X4) n comprises at least one sequence X6X7X8, wherein X6X7X8 is RAL or RLA, preferably RAL, and wherein this sequence is preferably located in the N-terminal amino acids of positions 4-7, and / or (ii) (X4) nX5 comprises at least one sequence X6X7X8, wherein X6X7X8 is EAL or ELA, preferably EAL, and wherein this sequence is preferably not located in the N-terminal amino acids of positions 1-6, and / or (iii) (X4) n X5 comprises at least one sequence X6X7X8, where X6X7X8 is QAL or QLA, preferably QAL. [5] Washing or cleaning agent according to one of the preceding claims, wherein the peptide (A) consists of at least 60% and increasingly preferably at least 61%, 62%, 63%, 64%, 65%, 66%, 67%, 68%, 69%, 70%, 71%, 72%, 73%, 74%, 75% of amino acids with a high alpha-helix-forming potential, wherein these amino acids are preferably selected from E, A, L, M, Q, K, R, F, I, H, and D, more preferably E, A, L, M, Q, K, R, F, I and H, even more preferably E, A, L, M, Q, K, R and F. [6] Washing or cleaning agent according to one of the preceding claims, wherein the at least one peptide conjugate has the following structure in N- to C-terminal orientation: (i) Z1Z3Z4Z5Z7, (ii) Z2Z3Z4Z5Z6, (iii) Z1Z3Z4Z5Z6, (iv) Z2Z3Z4Z5Z7, (V) Z1Z3Z4, (vi) Z2Z3Z4, (vii) Z4Z5Z7, and (viii) Z4Z5Z6, wherein Z1 to Z7 are as defined in claim 1. [7] Washing or cleaning agent according to one of the preceding claims, wherein the linker is selected from flexible linkers and rigid linkers, and / or wherein the at least one linker is selected from (I) (GGGGS) n with n = 1, 2, 3, or 4; (II) (G)6; (III) (G)8; (IV) (EAAAK) n with n = 1, 2, or 3; (V) A(EAAAK)4ALEA(EAAAK)4A; (VI) PAPAP; (VII)AEAAAKEAAAKA; and (VIII) (AP) nwith n = 10-34; preferably the linker is a linker having an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences recited in SEQ ID NO:29-40. [8] Washing or cleaning agent according to one of the preceding claims, wherein the at least one peptide and / or peptide conjugate is suitable for adhesion and / or binding to textiles. [9] Washing or cleaning agent according to one of the preceding claims, wherein the at least one peptide and / or peptide conjugate has a soil-repellent and / or soil-removing effect. [10] Peptide conjugate comprising in N- to C-terminal orientation the following sequence: (Z1)p(Z2)q(Z3)r(Z4)s(Z5)t(Z6)v(Z7)w, wherein Z4 is a peptide, preferably a textile-binding peptide, selected from (A) a peptide with the following amino acid sequence: (C)mX1X2X3(X4)nX5(C)o, where C is the amino acid cysteine, where m+o = 0 or 1; where X1 is a positively charged amino acid, preferably R or K, more preferably R, X2 and X3 are uncharged amino acids, preferably A, L, S, I, M or Q, more preferably A, S, I or L, particularly preferably A or L, each X4 independently of one another is any amino acid, preferably with the exception of P, more preferably with the exception of P and G, X5 is any positively charged or uncharged amino acid, preferably R or an uncharged amino acid, more preferably Q, A or L, particularly preferably A or L, m and o are 0 or 1, where n is an integer from 0 to 46, preferably 6 to 20, more preferably 6 to 12, particularly preferably 8 to 12, (B) a peptide having an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NO: 1-27, where s = 1; where Z1 and Z7 are independently -(C2H4O) k where k = 5-100, p and w are 0 or 1 and p+w = 0 to 2; wherein Z2 and Z6 are independently a peptide, preferably a textile-non-binding peptide, which has an amino acid sequence which has at least 80% and increasingly preferably at least 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 99.5% or 100% sequence identity with the amino acid sequence given in SEQ ID NO:28, wherein q and v are 0 or 1 and q+v = 0 to 2; wherein Z3 and Z5 are linkers, preferably peptide linkers, wherein r and t are 0 or 1 and r+t = 0 to 2; where p+q+r+t+v+w = 2 to 6, preferably 3 to 5, particularly preferably 3 or 4, most preferably 4. [11] Washing or cleaning agents, preferably textile washing agents, comprising at least one peptide conjugate according to claim 10. [12] Process for cleaning textiles and / or hard surfaces, in particular dishes, characterized by that in at least one process step a washing or cleaning agent according to one of claims 1 to 9 or 11 is used, wherein the process is preferably carried out in a temperature range of about 20°C to about 60°C, particularly preferably about 20°C to 40°C. [13] Use of a washing or cleaning agent according to one of claims 1 to 9 or 11 for cleaning textiles and / or hard surfaces, in particular dishes, preferably in a temperature range of about 20°C to about 60°C, particularly preferably about 20°C to 40°C. [14] Use of a peptide and / or peptide conjugate as a soil-repellent and / or soil-removing active ingredient, preferably in a temperature range of about 20°C to 60°C, particularly preferably about 20°C to 40°C, wherein the peptide and / or peptide conjugate is as defined in any one of the preceding claims. [15] Use of a peptide and / or peptide conjugate as defined in any one of the preceding claims in a washing or cleaning agent for improving the cleaning performance of the washing or cleaning agent on greasy and oily soils, preferably in a temperature range of about 20°C to 60°C, particularly preferably about 20°C to 40°C.