Peptides with dirt-releasing effect for detergents and cleaning agents

Abstract

The invention relates to peptides and / or peptide conjugates as described herein. The invention also relates to detergents 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 the aforementioned detergent or cleaning agent and to the use of a peptide and / or peptide conjugate as a dirt-releasing and / or dirt-repelling active ingredient in the washing and / or cleaning of textiles and / or hard surfaces, and for improving the cleaning performance of a detergent or cleaning agent containing said peptide and / or peptide conjugate.

Description

[0001] Henkel AG & Co. KGaA Dr. Dieckmann / RJL 2022P00281WO PEPTIDES WITH SOIL-REMOVING EFFECT FOR WASHING AND CLEANING AGENTS DESCRIPTION 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 further relates to a method for cleaning textiles and / or hard surfaces using the said washing or cleaning agent and the use of a peptide and / or peptide conjugate as a soil-removing and / or soil-repellent active ingredient when washing and / or cleaning textiles and / or hard surfaces, and for improving the cleaning performance of a washing or cleaning agent containing this peptide and / or peptide conjugate. Intensive research is being conducted on 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. For such surfaces, those with low surface energies, as often found in certain plastics, are particularly problematic. Such plastics are also referred to in the prior art as low surface energy polymers (LSEP) and include, for example, many polyolefins or polymers with ester functions. It is known to use "soil release polymers" to improve soil release or "soil repellent polymers" to prevent / reduce soil deposition in detergents for cleaning textiles.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 soil 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 influence on the ability of oil and grease to be washed out of textiles. This effect is particularly evident when a textile that has already been washed several times with an SRP polymer-containing agent is soiled.Accordingly, 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, e.g., polypropylene terephthalate. However, these polymers are typically not biodegradable. Therefore, there is a need for alternative or improved, particularly biodegradable SRP polymers for use in detergents and cleaning agents, and / or alternatives thereto. It has now surprisingly been found that certain peptides and / or peptide conjugates can represent a biodegradable alternative to SRP polymers. Of particular note here are peptides with a hydrophobic end and a hydrophilic end, where the hydrophobic part can bind to the textile while the hydrophilic part cannot.Particularly advantageous peptides can adhere to plastic surfaces, preferably LSEP (low surface energy polymers) surfaces, and especially 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 or cleaning agents, by providing a biodegradable alternative. They could also contribute to the stabilization of other ingredients.The invention therefore relates in a first aspect to a washing or cleaning agent, preferably 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, which is selected from (A) a peptide having the following amino acid sequence: (C). m X1X2X3(X4) n X5(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 which has an amino acid sequence which is 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,has 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, more preferably k = 30-75, more preferably k = 40-60, most 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, preferably 3 to 5, particularly preferably 3 or 4,very particularly preferably 4. In various embodiments - the peptide (A) is a peptide, wherein (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 no G and even more preferably also no Y; and / or - the peptide (A) is one, wherein (i) the sequence X1X2X3 is RSI, RAL or RLA, preferably RSI or RAL; and / or (ii) (X4), nX5 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) n at least one aromatic amino acid, preferably W or F; and / or - the peptide (A) is a peptide, 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) nX5 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% 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 where 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)n with n = 1, 2, or 3;(V) A(EAAAK)4AAA(EAA)4A; (VI) THE POPE; (VII) AEAAREABLE; und (VIII) (AP); nwith n = 10-34, preferably the linker is a linker 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 one of the amino acid sequences mentioned in SEQ ID NO: 29-40. It is particularly preferred that the at least one peptide and / or peptide conjugate is suitable for adhesion and / or binding to textiles. It is particularly preferred that the at least one peptide and / or peptide conjugate has a soil-repellent and / or soil-removing effect. 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.In preferred embodiments, the washing or cleaning agent according to the invention is a textile washing agent. 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, and particularly preferably about 8 to about 9. 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 having the following amino acid sequence: (C)mX1X2X3(X4)nX5(C)o, wherein 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 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 one of the amino acid sequences listed in SEQ ID NO: 1-27, where s = 1; where Z1 and Z7 independently of one another are -(C2H4O), kwhere 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. Further objects of the invention relate to - a method for cleaning textiles and / or hard surfaces, in particular dishes, characterized inthat in at least one process step, a washing or cleaning agent described herein is used, wherein the process is preferably carried out in a temperature range from about 20°C to about 60°C, particularly preferably from 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 from about 20°C to about 60°C, particularly preferably from 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 from about 20°C to about 60°C, particularly preferably from 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 from 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 from 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 from about 20°C to about 60°C, particularly preferably about 20°C to about 40°C. 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. Unless otherwise stated, all percentages are by weight (wt%), based on the total weight of the respective composition or agent. Numerical ranges given in the format "from x to y" include the stated values. Where multiple preferred numerical ranges are given in this format, it is to be understood that any ranges resulting from the combination of the various endpointsare also included. "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 specifications, 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 specified amount of the corresponding compounds. All quantity specifications stated in connection with the washing or cleaning agents described herein refer, unless otherwise stated,to wt.%, each based on the total weight of the composition. Furthermore, such quantities referring to at least one component always refer to the total amount of that component 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. "Approximately" or "approximately," as used herein with reference to numerical values, means the corresponding value ±10%, preferably ±5%. 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. "Substantially free of," 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. "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 for them to have a yield point. A substance, e.g., a composition or agent, is solid according to the definition of the invention if it is in the solid state at 25°C and 1,013 mbar. A substance, e.g., a composition or agent, is liquid according to the definition of the invention,when it is in the liquid state at 25°C and 1,013 mbar. Liquid also includes gelatin. 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 that has a free amino group. 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 that has a free carboxyl group. The expression "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. References herein to various interconnected or individual amino acid sequences are, unless otherwise stated.always shown in N- to C-terminal orientation. Furthermore, the individual amino acids or amino acid sequences are linked to one another via peptide bonds, unless otherwise stated. Accordingly, the hyphen in the peptide-linker-peptide representation, for example, means that these three corresponding sequences are fused to one another via peptide bonds. In the context of this invention, "adhesion" or "adhesive" is understood to mean an interaction between a peptide and / or peptide conjugate and a surface, whereby the peptide and / or peptide conjugate can adhere to the surface. Thus, the term "adhesion-promoting" refers to the ability, under suitable conditions, i.e., usually non-denaturing conditions, to interact with various surfaces, e.g., textile surfaces, and / or to adhere to a specific surface, with a binding affinity greater than that of a reference sequence or a reference molecule.which has no 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. 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 can be in the range of 80% relative to the total length of the parent peptide, and can 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%. The present invention is based on the surprising finding of the inventors that certain peptides and / or peptide conjugates when used in washing or cleaning agents not only provide improved cleaning performance on greasy and / or oily soils,but also exhibit a soil-removing and / or soil-repellent effect. They thus 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 especially textiles made of (LSEP) plastic or with an (LSEP) plastic content. 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 the textiles. Furthermore, they could contribute to reducing or completely eliminating synthetic and chemical substances, e.g., in detergents or cleaning agents.by representing a biodegradable alternative. They could also contribute to the stabilization of other ingredients. This is particularly surprising given that such peptides and / or peptide conjugates have so far been associated neither with a soil-removing and / or soil-repellent effect nor with improved cleaning performance of washing or cleaning agents, in particular not with regard to greasy and / or oily soils. Textile-binding peptides 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 has the following 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, 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 is 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. 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, 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. 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 is independently 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. Alternatively or additionally, the peptide comprises or consists of an amino acid sequence which is 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. 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 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) ofor 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 the sequence is listed in N- to C-terminal orientation unless otherwise stated. Peptides can, in various embodiments, be chemically synthesized and / or recombinantly produced by protein design. Short peptides are now easily synthesized, e.g., by solid-phase synthesis. Longer peptides and polypeptides, on the other hand, are often also produced recombinantly in the host organism. Typical acidic or negatively charged amino acids (depending on the pH) are D and E. Positively charged or basic amino acids (depending on the pH) typically include R, K, and H. 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.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 have helix-breaking properties and can therefore adversely affect the secondary structure of the peptides. 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.In preferred embodiments, the peptide according to the invention has: (i) a total charge of -2 to +12, preferably 0 to +8, more preferably 0 to +4, particularly 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) a negative or neutral net charge at the C-terminus, which comprises the last 3-6 amino acids, preferably at least one negatively charged amino acid, in particular E; and / or (iv) no P and more preferably also no G and in particular also no Y. All of the aforementioned features, in particular (i)-(iv), can be realized individually or in any combination. 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, for example,is fulfilled if the N-terminal 3-4 amino acids have 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. The feature that the peptide has a negative or neutral net charge at the "C-terminus, which comprises 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, for example, EAL or the double sequence of this motif. In various preferred embodiments, the sequence is X1X2X3RAL, RSI, or RLA, preferably RAL or RLA, in particular 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. Furthermore, it is preferred that (i) the sequence (X4)nX5 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, independently of one another, are 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). nat least one aromatic amino acid, preferably W or F. If the sequence X6X7X8 comprises 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 may comprise one or more further sequences X6X7X8 which are C-terminal to the sequence comprising a positively charged amino acid as X6, wherein these further sequences then preferably do not have a positively charged amino acid as X6. It is preferred that one of the sequences X6X7X8 which are close, i.e. within the 6 C-terminal amino acids, or at the C-terminus, has a negatively charged amino acid as X6, e.g. E.If, in some embodiments, the peptide contains an aromatic amino acid selected from W and F, a positively or negatively charged amino acid is located next to it, particularly at the C-terminal side; in particular, no other aromatic amino acid is located next to the aromatic amino acid. 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 the peptide sequence in various embodiments because it has helix-breaking properties. In various embodiments, the peptide is therefore free of Y residues. In the context of the present invention, "pi-stacking" refers to the non-covalent interaction between aromatic ring systems. Preferably, (i) comprises (X4). nat 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 or at least 6-7 amino acids away 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)nX5 comprises at least one sequence X6X7X8, wherein X6X7X8 is EQA, QAL, LQA, or QLA, preferably EQA, QAL, or QLA, in particular QAL. In other possible embodiments, (X4) comprises nX5 comprises at least one sequence X6X7X8, where X6X7X8 is QLA or EQA, which sequence is preferably not located in the N-terminal amino acids of positions 1-6 or 1-11. It is further possible that (X4)nX5 comprises at least one sequence X6X7X8X9, where X6X7X8X9 is AQLA or SEQA, which sequence is preferably not located in the N-terminal amino acids of positions 1-6 or 1-11. In preferred embodiments, the peptide comprises the sequence X1X2X3, where X1X2X3 is RAL, and (X4)nX5 comprises at least one of QAL and EAL, preferably both. In such embodiments, the peptide has the sequence (C) m RAL(X 10 ) q QAL(X 11 ) r EAL(X 12 ) s (C) oor (C)mRAL(X10)qEAL(X11)rQAL(X12)s(C)o, where X10 and X11 are independently any amino acid, preferably with the exception of P, more preferably with the exception of P and G, X12 is 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. Furthermore, it is preferred that the peptide additionally comprises at least one further (second) sequence RAL. In various embodiments, this can directly follow the first RAL sequence C-terminally or be separated from it by 1-3 amino acids, e.g., by 1, 2, or 3 amino acids. In preferred embodiments, the peptide contains two RAL sequences and at least one EAL and one QAL sequence each.Preferred sequences are: ^ RALRAL(X10)qQAL(X11)rEAL(X12)s, ^ RALRAL(X10)qEAL(X11)rQAL(X12)s, ^ RAL(X10)qRALQAL(X11)rEAL(X12)s, ^ RAL(X10)qRALEAL(X11)rQAL(X12)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 X10 and X11 are independently 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 12is 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. Furthermore, in various embodiments it is preferred that the peptide contains at least one W or F, preferably exactly one W or F. 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; particularly preferably from E, A, L, M, Q, K, R and F. 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% 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 from E, A, L, M, Q, K, R, F, I and H; particularly preferably from E, A, L, M, Q, K, R and F. 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. 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 indicated 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. 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. Preferably, the peptide has an amino acid sequence having 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,For example, it has 12 to 18 amino acids. 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. 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),^ RALRALQALEALEAL (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). Variants of the peptides according to the invention, the amino acid sequence of which is 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 corresponding 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 corresponding to the sequences in SEQ ID NO:1-27. For example, if 1 position differs, either one of the amino acids of the respective sequence may have been exchanged, or the sequences may be identical, but an amino acid within the amino acid chain or at the N- or C-terminal end has been added or omitted. For example, a cysteine ​​(C) could have been added at the C- or N-terminal end. The peptide according to the invention particularly preferably has a sequence shown in SEQ ID NO:1-27. The peptide particularly preferably 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. Peptides particularly preferred according to the invention are textile-binding peptides, i.e., peptides that have the ability to adhere to textile surfaces under suitable conditions, i.e., usually non-denaturing conditions, and thus exhibit adhesive properties. Good adhesion to textile surfaces, especially textile surfaces made of synthetic fibers, such as polyester-containing textiles, can be achieved, for example, by a peptide with a pronounced helix structure (especially alpha-helix structure) and / or a high arginine content, especially at one of the termini. Preferred peptides that exhibit good adhesion, especially to plastics, preferably polyester, have an amino acid sequence,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% or 100% sequence identity to one of the amino acid sequences given in SEQ ID NO: 1-27. Particularly preferred peptides, which in particular Plastic, preferably polyester, exhibit good adhesion, have an amino acid sequence that 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 exhibit good adhesion, in particular to plastic, preferably polyester, have an amino acid sequence that is identical to one of the amino acid sequences given in SEQ ID NO: 1-27. 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 that 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 exhibit good adhesion to plastic-containing, preferably polyester-containing textiles, have an amino acid sequence that is identical to one of the amino acid sequences given in SEQ ID NO:1-27. Preferred peptides that are textile-binding within the meaning of the invention and exhibit good adhesion to plastic-containing, preferably polyester-containing textiles. Synthetic-containing blended fabrics, preferably polyester-containing blended fabrics, in particular polyester / cotton blended fabrics, exhibit good adhesion, have an amino acid sequence that 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 that are textile-binding within the meaning of the invention and exhibit good adhesion to synthetic-containing blended fabrics, preferably polyester-containing blended fabrics, in particular polyester / cotton blended fabrics,exhibit 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 blended fabrics, preferably polyester-containing blended fabrics, in particular polyester / cotton blended fabrics, have an amino acid sequence which is identical to one of the amino acid sequences given in SEQ ID NO: 1-27. Methods for determining adhesion are known to those skilled in the art, and any suitable method can be used. A common method for determining adhesion is based on a direct measurement method using µBCA. For this purpose, cloth patches are coated with a peptide solution to be tested (0.0.2 mg / ml in distilled water), incubated for 1 h at room temperature while 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 read from the measured adhesion values. AP in % shows what percentage of the applied amount (100%) remains on the cloth after washing. The higher the AP value,the higher the binding affinity and thus the adhesion. (<20% = no adhesion; 21 to 40% = low adhesion; 41 to 60% = medium adhesion; 61 to 80% = good adhesion; >80% = very good adhesion). Another detection method for determining adhesion is based on the fluorescence method described here in the examples. Other methods for determining adhesion known to the person skilled in the art can also be used. A peptide is a textile-binding peptide within the meaning of the invention if, in one of the methods mentioned, the ability of the peptide to adhere to textile surfaces is demonstrated, wherein the binding affinity is greater than that of a reference molecule, and wherein 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.which was not developed for this purpose and does not meet the sequence specifications described herein. A peptide is, in particular, a textile-binding peptide within the meaning of the invention if, in a method according to Example 2, the ability of the peptide to adhere to textile surfaces is demonstrated, wherein the binding affinity is greater than that of a reference molecule. A peptide is, in particular, also a textile-binding peptide within the meaning of the invention if, in a previously described BCA method, the ability of the peptide to adhere to textile surfaces is demonstrated, wherein the AP value is greater than 61% and preferably greater than 80%. Textile-nonbinding peptide Alternatively or additionally, the washing or cleaning agent according to the invention comprises at least one peptide conjugate, wherein the peptide conjugate may contain a textile-nonbinding peptide. In this context, "textile-nonbinding" meansthat textile-non-binding peptides do not have the ability to adhere to textile surfaces. 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. Very particularly preferably, the textile-non-binding peptide has the following amino acid sequence: ^ NGLLIPQFLVAS (SEQ ID NO: 28). 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,wherein the binding affinity is lower than or equal to that of a reference molecule. A peptide is, within the meaning of the invention, in particular a textile-nonbinding peptide 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. A peptide is, within the meaning of the invention, in particular also a textile-nonbinding peptide if, in a previously described BCA method, the ability of the peptide to adhere to textile surfaces is not demonstrated, wherein the AP value is less than 20%. Peptide conjugate 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 having the following amino acid sequence: (C)mX1X2X3(X4)nX5(C)o, wherein 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 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 one of the amino acid sequences mentioned 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, most 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, 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 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,where 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. According to the invention, the peptides contained in the peptide conjugate according to the invention are as defined above, namely textile-binding peptides and / or textile-nonbinding peptides. 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." 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-non-binding peptides, as defined herein. More preferably, the peptide conjugate contains one textile-binding peptide and two textile-non-binding peptides. In various embodiments, if 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. In various embodiments, if more than one textile-non-binding peptide is present in the peptide conjugate, these may be the same or different. In preferred embodiments, they are the same. 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. 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 are e.g. lysine (ε-amino group),Histidine (imidazole side chain) or aspartic acid / glutamic acid (carboxyl groups). PEGylation can be achieved through 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. A 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 addition of polyethylene glycol maleimide to the OH group of any terminal amino acid. 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, 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. 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, 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, 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. 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. 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, particularly preferably about 40 to about 60 ethylene glycol units,very particularly 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, particularly preferably about 1760 g / mol to about 2640 g / mol, very particularly preferably about 2000 g / mol. In various embodiments of the invention, the PEG group and / or the at least one, preferably at least two, textile-nonbinding 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 a 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. 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 art (Chen et al. (2013) Fusion protein linkers: Property, design and functionality, Advanced Drug Delivery Reviews, 65 (10): 1357-1369). If the peptide conjugate according to the invention comprises at least one linker,then 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, where Z4 is a peptide, preferably a textile-binding peptide, selected from (A) a peptide having the following amino acid sequence: (C), m X1X2X3(X4) n X5(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 is independently 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 which has an amino acid sequence which is 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,has 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, more 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, independently of one another, are 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. 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, where Z4 is a peptide, preferably a textile-binding peptide, selected from (A) a peptide having 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 is independently 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 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 one of the amino acid sequences mentioned in SEQ ID NO:1-27, where s = 1; where Z1and Z7independently represent –(C2H4O), kwhere 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. If the linker is, as preferred, a peptide linker,then the respective first or last amino acid of the peptide is linked via a peptide bond to the respective first or last amino acid of the peptide linker. If the peptide conjugate comprises a peptide linker and a PEG group, then PEGylation is carried out 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. 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. 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. 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 exhibit its functionality, i.e. as a bond between peptides and / or peptide and PEG chain can function,without impairing the advantageous properties of corresponding peptide conjugates as described and disclosed herein. Linkers preferred according to the invention have one of the following amino acid sequences: ^ GGGGS (SEQ ID NO: 29), ^ GGGGSGGGGS (SEQ ID NO: 30), ^ GGGGSGGGGSGGGGS (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), ^ AEAAAKEAAAKEAAAKEAAAKALEAEAAAKEAAAKEAAAKA (SEQ ID NO: 38), ^ PAPAP (SEQ ID NO: 39) or ^ AEAAAKEAAAKA (SEQ ID NO: 40). Particularly preferred is the linker having the following amino acid sequence: ^ GGGGSGGGGSGGGGS (SEQ ID NO:31) or ^ EAAAKEAAAKEAAAK (SEQ ID NO:37). 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 having 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 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 one of the amino acid sequences listed in SEQ ID NO:1-27, where s = 1; where Z1 and Z7 independently of one another are -(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 peptide linkers, wherein the peptide linker is selected from the group consisting of (I) (GGGGS) nwith 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; 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. 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-nonbinding 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-non-binding peptide – linker (II) – textile-binding peptide – linker (II) – textile-non-binding peptide, (xi) PEG – linker (II) – textile-binding peptide – linker (II) – textile-non-binding peptide, (xii) textile-non-binding peptide – linker (II) – textile-binding peptide – linker (II) – PEG, (xiii) PEG – linker (II) – textile-binding peptide, (xiv) textile-non-binding peptide – linker (II) – textile-binding peptide, (xv) textile-binding peptide – linker (II) – PEG, (xvi) textile-binding peptide – linker (II) – textile-nonbinding 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-nonbinding peptide,(xx) textile-non-binding peptide – linker (III) – textile-binding peptide – linker (III) – PEG, (xxi) PEG – linker (III) – textile-binding peptide, (xxii) textile-non-binding 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-non-binding peptide – linker (IV) – textile-binding peptide – linker (IV) – textile-non-binding peptide, (xxvii) PEG – linker (IV) – textile-binding peptide – linker (IV) – textile-non-binding peptide, (xxviii) textile-non-binding 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-nonbinding peptide,(xxxiii) PEG – linker (V) – textile-binding peptide – linker (V) – PEG, (xxxiv) textile-non-binding peptide – linker (V) – textile-binding peptide – linker (V) – textile-non-binding peptide, (xxxv) PEG – linker (V) – textile-binding peptide – linker (V) – textile-non-binding peptide, (xxxvi) textile-non-binding peptide – linker (V) – textile-binding peptide – linker (V) – PEG, (xxxvii) PEG – linker (V) – textile-binding peptide, (xxxviii) textile-non-binding 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, (xliii) PEG – linker (VI) – textile-binding peptide – linker (VI) – textile-nonbinding peptide,(xliv) textile-non-binding peptide – linker (VI) – textile-binding peptide – linker (VI) – PEG, (xlv) PEG – linker (VI) – textile-binding peptide, (xlvi) textile-non-binding 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, (l) textile-non-binding peptide – linker (VII) – textile-binding peptide – linker (VII) – textile-non-binding peptide, (li) PEG – linker (VII) – textile-binding peptide – linker (VII) – textile-non-binding peptide, (lii) textile-non-binding peptide – Linker (VII) – textile-binding peptide – Linker (VII) – PEG, (liii) PEG– Linker (VII) – textile-binding peptide, (liv) textile-nonbinding peptide – Linker (VII) – textile-binding peptide, (lv) textile-binding peptide – Linker (VII) – PEG chain, (lvi) textile-binding peptide – Linker (VII) – textile-nonbinding peptide,(lvii) PEG–linker (VIII) – textile-binding peptide – linker (VIII) – PEG, (lviii) textile-non-binding peptide – linker (VIII) – textile-binding peptide – linker (VIII) – textile-non-binding peptide, (lix) PEG–linker (VIII) – textile-binding peptide – linker (VIII) – textile-non-binding peptide, (lx) textile-non-binding peptide – linker (VIII) – textile-binding peptide – linker (VIII) – PEG, (lxi) PEG – linker (VIII) – textile-binding peptide, (lxii) textile-non-binding peptide – linker (VIII) – textile-binding peptide, (lxiii) textile-binding peptide – linker (VIII) – PEG, (lxiv) textile-binding peptide – linker (VIII) – textile-non-binding 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 having 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 is independently 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 is 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; wherein the textile non-binding peptide is 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 the amino acid sequence listed in SEQ ID NO:28. In preferred embodiments, the linker is selected from: ^ GGGGS (SEQ ID NO:29), ^ GGGGSGGGGS (SEQ ID NO:30), ^ GGGGSGGGGSGGGGS (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), ^ AEAAAKEAAAKEAAAKEAAAKALEAEAAAKEAAAKEAAAKA (SEQ ID NO:38),^ PAPAP ( SEQ ID NO:39 ) und ^ AEAAAKEAAAKA ( SEQ ID NO : 40 ); and / or the non-textile binding is derived from: ^ NGLLIPQFLVAS (SEQ ID NO:28); and / or the textile-binding Peptide derived from: ^ RALQALRALQALEAL (SEQ ID NO:1), ^ RALRALRALQALEAL (SEQ ID NO:2), ^ RALRALRALQALQAL (SEQ ID NO:3), ^ RALRALRALQALQAL (SEQ ID NO:4), ^ RALRALRALQALEAL (SEQ ID NO:5), ^ RALFEALQALFRALEAL (SEQ ID NO:6), ^ RALRALEALQALEA (SEQ ID NO:7), ^ RALFEALFRALEALR (SEQ ID NO:8), ^ RALFEALFRALFRALEAL (SEQ ID NO:9), ^ RALLEALFRALEAL (SEQ ID NO:10), ^ RALRALEALQALEA (SEQ ID NO:11), ^ RALFEALFRALQALEA (SEQ ID NO:11). NO:12), ^ RALEALWRALEAL (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:17). 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). 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-nonbinding peptide is 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), ^ RALRALQALEALEAL (SEQ ID NO:5), ^ RALFEALQALFRALEAL (SEQ ID NO:6), ^ RALRALALEALQALEA (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). In most preferred embodiments, the linker is selected from: ^ GGGGS (SEQ ID NO:29); and the textile non-binding peptide is 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). In further preferred embodiments, the linker is selected from: ^ GGGGS (SEQ ID NO:29); and the textile-non-binding peptide is selected from: ^ NGLLIPQFLVAS (SEQ ID NO:28); and the textile-binding peptide is selected from: ^ RALQALRALQALEAL (SEQ ID NO:1). In further preferred embodiments, the linker is selected from: ^ GGGGS (SEQ ID NO:29); and the textile-non-binding peptide is selected from: ^ NGLLIPQFLVAS (SEQ ID NO:28); and the textile-binding peptide is selected from: ^ RALRALQALEALEAL (SEQ ID NO:5). In further preferred embodiments, the linker is selected from: ^ GGGGS (SEQ ID NO:29); and the textile-non-binding peptide is selected from: ^ NGLLIPQFLVAS (SEQ ID NO:28); and the textile-binding peptide selected from: ^ RSIVTFSLRQNR (SEQ ID NO:25). Most preferred peptide conjugates include: ^ (PEG)-GGGGS-RSIVTFSLRQNR-GGGGS-(PEG) (SEQ ID NO:41), ^ (PEG)-GGGGS-RALQALRALQALEAL-GGGGS-(PEG) (SEQ ID NO:42),^ (PEG)-GGGGS-RALRALQALEALEAL-GGGGS-(PEG) (SEQ ID NO:43), ^ NGLLIPQFLVAS-GGGGS-RSIVTFSLRQNR-GGGGS-NGLLIPQFLVAS (SEQ ID NO:44), ^ NGLLIPQFLVAS-GGGGS-RALQALRALQALEAL-GGGGS-NGLLIPQFLVAS (SEQ ID NO:45), and ^ NGLLIPQFLVAS-GGGGS-RALRALQALEALEAL-GGGGS-NGLLIPQFLVAS (SEQ ID NO:46). The identity of nucleic acid or amino acid sequences is determined by sequence comparison. This sequence comparison is based on the state-of-the-art and commonly used BLAST algorithm (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 carried out in principle bythat similar sequences of nucleotides or amino acids in the nucleic acid or amino acid sequences are assigned to one another. A tabular assignment of the relevant positions is called 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 programs include the Clustal series (see, for example, Chenna et al. (2003) Multiple sequence alignment with the Clustal series of programs, Nucleic Acid Res., 31:3497-3500), T-Coffee (see, for example, 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. Furthermore, sequence comparisons (alignments) are possible using the computer program Vector NTI® Suite 10.3 (Invitrogen Corporation, 1600 Faraday Avenue, Carlsbad, California,USA) with the specified default parameters, whose AlignX module for sequence comparisons is based on ClustalW, or Clone Manager 10 (using 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. Such a comparison also allows a statement about the similarity of the compared sequences to each other. It is usually expressed as percent identity, i.e., the proportion of identical nucleotides or amino acid residues at the same 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 they usually perform 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 across entire polypeptides or genes or just across 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 have identical functions. They can be small and consist of only a few nucleotides or amino acids. Such small regions often perform essential functions for the overall activity of the protein. It can therefore be useful to limit sequence matches to individual,small regions if necessary. Unless otherwise stated, however, identity or homology statements in the present application refer to the total length of the respective nucleic acid or amino acid sequence indicated. 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). The person skilled in the art in the field of peptide and protein technology knows a variety of suitable methods for determining the peptide or protein concentration, which can be used in the context of this invention. Peptides according to the invention can have amino acid changes, in particular amino acid substitutions, insertions or deletions. Such peptides can be produced, for example, by targeted genetic modification, i.e. by mutagenesis methods.further developed and optimized for specific applications or with regard to special properties (e.g., with regard to their stability, binding, etc.). For example, targeted mutations such as substitutions, insertions, or deletions can be introduced into the known molecules in order to, for example, change certain properties. For this purpose, in particular the surface charges and / or the isoelectric point of the molecules and thus their interactions with a surface can be changed. For example, the net charge of the peptides can be changed in order to influence substrate binding. Alternatively or additionally, one or more corresponding mutations can, for example, increase the stability or adsorption of the peptide. Advantageous properties of individual mutations, e.g., individual substitutions, can complement each other. Thus, the invention also encompasses peptides characterized bythat they are obtainable from a peptide as described above as 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, the resulting peptide 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% and less than 100% sequence identity with one of the amino acid sequences according to SEQ ID NO:1-28. 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 one 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. In preferred embodiments, the peptide according to the invention can also be modified. Preferred modifications can be, for example, the coupling of 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. All of the aforementioned features and embodiments can be realized individually or in any combination. Furthermore, the peptide according to the invention can also be at least one subunit (module) of a larger peptide or polypeptide, wherein 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 comprising 100 or more amino acids. The term "larger peptides" preferably refers to peptides with at least 40 amino acids.unless otherwise described. 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 together 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 in a linear fashion via peptide bonds, optionally also via a spacer. The peptides described herein can, in various embodiments, have been chemically synthesized and / or recombinantly produced by protein design. Short peptides are now easily synthesized, e.g., via solid-phase synthesis such as the Merrifield solid-phase synthesis.Longer peptides and polypeptides, on the other hand, are often produced recombinantly in the host organism, e.g. in bacteria or yeasts. It is preferred to produce the peptides and / or peptide conjugates according to the invention by means of recombinant processes. This refers to all genetic engineering or microbiological processes which are based on the genes for the peptides of interest being introduced into a host organism suitable for production and being transcribed and translated by this host organism (summarized in the context of this invention as biotechnological processes). 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 have 1 to 30 peptide units (each according to the invention), each of which is separated by spacers of 1 to 10 amino acids in length (e.g. 1, 2,3 or 4 amino acids) are separated from each other. Alternatively, the spacers can also be or comprise cleavage sites for specific proteases / peptidases, in particular endopeptidases, or can form such cleavage sites together with parts of the peptide. It is possible for a person skilled in the art to use methods generally known today, such as chemical synthesis or the polymerase chain reaction (PCR) in conjunction with standard molecular biological and / or protein chemical methods, to produce the corresponding nucleic acids up to 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. In particularly preferred embodiments, the peptide and / or peptide conjugate described herein is produced by means of biotechnological processes, as described above.The at least one peptide and / or peptide conjugate according to the invention is preferably suitable for adhesion and / or binding to textiles, as described herein. 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, in particular through the 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, in particular in machine washing or hand washing. 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.%. In preferred embodiments, the washing or cleaning agent is a textile detergent. 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 (blended 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 blend thereof,Even more preferably polyester (PES), polyethylene (PE), polypropylene (PP), polystyrene (PS), copolymers or blends 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. The term "blend" or "blended 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 blend or blended fabric consists of cotton and at least one plastic, in particular polyester. In preferred embodiments, a textile with a plastic content or a plastic blend or blended 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%. 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. The washing and cleaning agents according to the invention include all conceivable types of washing or cleaning agents, both concentrates and undiluted agents, for use on a commercial scale, in the washing machine or for hand washing or cleaning. These include, for example, detergents for textiles, carpets, or natural fibers,for which the term "detergent" is used. These 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. This means, 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 that are added to the actual washing agent during manual or machine laundry to achieve an additional effect. Furthermore, the term "washing and cleaning agents" within the scope of the invention also includes textile pre- and post-treatment agents, i.e. agents with which the laundry is brought into contact before the actual washing, e.g., to loosen stubborn dirt.and also those agents which, in a step following the actual textile washing process, impart further desirable properties to the laundry, such as a pleasant feel, crease resistance, or low static charge. Fabric softeners are counted among the latter agents. This also includes agents for use in (semi-)automated washing or cleaning systems, such as robot mops or wet vacuum cleaners. The washing or cleaning agents according to the invention, which may be in the form of powdered or granular solids, in compacted or recompacted particle form, as homogeneous solutions or suspensions, may contain all known ingredients customary in such agents. The agents according to the invention may, in particular, contain 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, color transfer inhibitors, foam regulators, as well as dyes and fragrances. Advantageous ingredients of the inventive agents 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. Further embodiments of the invention include all solid, powdered, liquid, gel-like, or pasty dosage forms of the inventive agents, 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, especially 500 g / l to 900 g / l or 600 g / l to 850 g / l. Solid dosage forms of the product also include extrudates, granules, tablets, or pouches. Alternatively, the product can also be liquid, gel, or paste-like.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 detergents are generally preferred. Furthermore, the detergent can be present as a one-component system. Such detergents consist of a single phase. Alternatively, a detergent can also consist of several phases. Such a detergent is therefore divided into several components. In a preferred embodiment, the detergent according to the invention is a textile detergent. In a preferred embodiment, the detergent according to the invention is a liquid textile detergent. In a preferred embodiment, the detergent according to the invention is a solid textile detergent. Multi-phase formulations are not preferred within the scope of this invention, but are not excluded. The viscosity of the liquid detergents 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 type LVT or LVDV-II+ with small sample adapter at a speed of 30 min, -1, wherein the Brookfield spindle used as the measuring body is to 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 preferably used. 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). Suitable water-soluble polymer(s) are particularly polymers from the group of (optionally acetalized) polyvinyl alcohols (PVAL) and copolymers thereof.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 are marketed by MonoSol LLC, for example, under the designation M8630, M8720, M8310, C8400, or M8900. Also suitable are films with the designations Solublon® PT, Solublon® GA, Solublon® KC, or Solublon® KL from Aicello Chemical Europe GmbH, or the VF-HP films from Kuraray. 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.The agents according to the invention can contain one or more surfactants, with particular emphasis being given to anionic surfactants, nonionic surfactants, and mixtures thereof, but cationic, zwitterionic, and / or amphoteric surfactants can also be present. The agents preferably contain 5 to 70% by weight, more preferably 35 to 60% by weight, and more preferably 40 to 55% by weight of surfactant. Suitable anionic surfactants are, in particular, soaps and those containing sulfate or sulfonate groups, preferably with alkali ions as cations. Suitable soaps are preferably the alkali metal 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. Suitable sulfate-type surfactants include the salts of the sulfuric acid half-esters of C12-18 fatty alcohols and the sulfation products of the aforementioned non-ionic surfactants 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, C12-18-olefinsulfonates, which are formed by the reaction of corresponding monoolefins with sulfur trioxide, mixtures of alkene and hydroxyalkanesulfonates, disulfonates, as can be obtained, e.g. 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 ^-sulfofatty acid esters (estersulfonates) which are formed during the sulfonation of fatty acid methyl or ethyl esters, e.g. ^-sulfonated methyl esters of hydrogenated coconut, palm kernel, or tallow fatty acids. The agent preferably contains 2 to 55% by weight, preferably 3 to 35% by weight, of anionic surfactant. Most preferably, the agent contains 3 to 25% by weight of alkylbenzenesulfonate. In addition, the agent can preferably contain further anionic surfactants, in particular alkyl ether sulfates, and nonionic surfactants, in particular fatty alcohol alkoxylates. These can then make up the remainder of the surfactants. Suitable alkylbenzenesulfonates are preferably selected from linear or branched alkylbenzenesulfonates of the formula - + Na , H or alkyl and together contain 6 to 19, preferably 7 to 15 and in particular 9 to 13 C atoms. A particularly preferred representative is sodium dodecylbenzylsulfonate. The alkali metal salts and in particular the sodium salts of the sulfuric acid monoesters 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 C12-15 alkyl sulfates as well as C14-15 alkyl sulfates are preferred. Sulfuric acid monoesters of the straight-chain or branched C alkyl sulfates ethoxylated with 1 to 6 mol of ethylene oxide are also preferred. 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. Suitable alkyl ether sulfates are, for example, compounds of the formula R 1 -O-(AO)n-SO3- X + . 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 R1 are derived from C 12-18 -Fatty alcohols, e.g., coconut fatty alcohol, tallow fatty alcohol, lauryl, myristyl, cetyl, or stearyl alcohol, or C10-20 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 mixtures thereof. In various embodiments, the alkyl ether sulfate can be selected from fatty alcohol ether sulfates of the formula O - Particularly preferred representatives are Na-C 12-14- Fatty 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 have a narrow homolog distribution (narrow range ethoxylates, NRE). It has proven advantageous for cold wash performance if the products also contain soap(s). Preferred products are therefore characterized by the fact that they contain 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.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. As non-ionic surfactants, preferably alkoxylated, advantageously ethoxylated, in particular 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 are used, in which the alcohol radical can be linear or preferably methyl-branched in the 2-position.The mixture can contain linear and methyl-branched residues, as is usually the case with oxo alcohol residues. However, alcohol ethoxylates with linear residues 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, C12-14 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 C 12-18- 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 of these are tallow fatty alcohol with 14 EO, 25 EO, 30 EO, or 40 EO. 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 with 1 to 4 carbon atoms in the alkyl chain, in particular fatty acid methyl esters. Another class of nonionic surfactants that can be used advantageously are alkyl polyglycosides (APG).Usable alkyl polyglycosides satisfy the general formula RO(G). zin which R is 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 is the symbol which stands for 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. Preference is given to using linear alkyl polyglycosides, i.e. alkyl polyglycosides in which the polyglycosyl radical is a glucose radical and the alkyl radical is an n-alkyl radical. Non-ionic surfactants of the amine oxide type, e.g. N-cocoalkyl-N,N-dimethylamine oxide and N-tallowalkyl-N,N-dihydroxyethylamine oxide, and of the fatty acid alkanolamide type may also be suitable. The amount of these non-ionic surfactants is preferably not more than that of the ethoxylated fatty alcohols, in particular not more than half of that. Suitable amphoteric surfactants are, for example, betaines of the formula (Riii )(R iv )(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 C11-17-alkylamidopropyldimethylcarboxymethylbetaine. 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 ixstands for four identical or different, in particular two long-chain and two short-chain, alkyl radicals and X- stands for an anion, in particular a halide ion, e.g. didecyldimethylammonium chloride, alkylbenzyldidecylammonium chloride and mixtures thereof. Other suitable cationic surfactants are quaternary surface-active compounds, in particular with a sulfonium, phosphonium, iodonium or arsonium group, which are also known as antimicrobial agents. By using quaternary surface-active compounds with antimicrobial action, the agent can be given an antimicrobial effect or its antimicrobial effect, which may already be present due to other ingredients, can be improved. 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 complex-forming 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). Preferred aminoalkanephosphonates are ethylenediaminetetramethylenephosphonate (EDTMP), diethylenetriaminepentamethylenephosphonate (DTPMP), and their higher homologues. They are preferably used in the form of the neutral sodium salts, e.g., the hexasodium salt of EDTMP or the hepta- and octasodium salts of DTPMP. HEDP from the phosphonate class is preferred as a builder.The aminoalkanephosphonates also have a pronounced heavy metal binding capacity. Accordingly, it may be preferable, especially if the agents also contain bleach, to use aminoalkanephosphonates, in particular DTPMP, or mixtures of the aforementioned phosphonates. 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 which contain 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. 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 to 8.0 wt.%, preferably 0.2 to 5.0 wt.%, more preferably 0.3 to 3.0 wt.%, and particularly preferably 0.5-2.0 wt.%. In further preferred embodiments, the washing and / or cleaning agents according to the invention are essentially free of phosphonate-containing compounds. "Essentially free of phosphonate-containing compounds" in this context means that the corresponding agent contains less than 2 wt.%-%, preferably less than 1 wt.%, more preferably less than 0.5 wt.% and particularly preferably less than 0.1 wt.%, of phosphonate-containing compounds, based on the total weight of the agent. In particularly preferred embodiments, these agents are free of phosphonate-containing compounds. The agents according to the invention further preferably contain builders, preferably at least one water-soluble and / or water-insoluble, organic and / or inorganic builder. The builders include in particular silicates, carbonates and organic cobuilders. Organic cobuilders that can be mentioned in particular are polycarboxylates / polycarboxylic acids, polymeric polycarboxylates, aspartic acid, polyacetals, dextrins, other organic cobuilders and phosphonates. These classes of substance are described below. Organic cobuilder substances can, if desired, be used 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, and citrate in the form of trisodium citrate dihydrate. Polymeric polycarboxylates are also suitable as builders, for example:the alkali metal salts of polyacrylic acid or polymethacrylic acid, e.g., those with a relative molecular weight of 500 to 70,000 g / mol. For the purposes of this application, the molar masses stated for polymeric polycarboxylates are weight-average molar 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 molar weight values. These figures differ significantly from the molar weight figures used for polystyrenesulfonic acids as a standard. The molar masses measured against polystyrenesulfonic acids are generally significantly higher than the molar masses stated in this application. Suitable polymers are, in particular, polyacrylates, which preferably have a molar mass of 2,000 to 20,000 g / mol.Due to their superior solubility, the short-chain polyacrylates from this group, which have molecular weights of 2000 to 10,000 g / mol, and particularly preferably of 3000 to 5000 g / mol, may again be preferred. 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. A solid agent 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 organic framework substances mentioned above.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, in particular amorphous sodium silicates, with a molar ratio Na2O:SiO2 of 1:2 to 1:2.8. As crystalline silicates, which can be present alone or in a mixture with amorphous silicates, preference is given to using crystalline phyllosilicates of the general formula Na2SiO2x+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 phyllosilicates are those in which x in the general formula mentioned assumes the values ​​2 or 3. In particular, both β- and δ-sodium disilicates (Na2SiO5 ^ y H2O) are preferred. Practically anhydrous crystalline alkali silicates of the above-mentioned general formula, in which x is a number from 1.9 to 2.1, produced from amorphous alkali silicates, can also be used in agents according to the invention.In a further embodiment of the inventive compositions, 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 inventive compositions. In compositions 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^ x H2O, magadiite), Na-SKS-3 (Na2Si8O17 ^ x H2O) or Na-SKS-4 (Na2Si4O9 ^ x H2O, makatite). Of these, Na-SKS-5 (^-Na2Si2O5), Na-SKS-7 (ß-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 layered silicate and citrate, of crystalline layered silicate 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 compositions according to the invention in amounts of 1 to 20 wt.%, in particular 5 to 15 wt.%.Other important water-soluble inorganic builder substances are carbonates (and hydrogen carbonates), especially sodium carbonate, and phosphonic acids / phosphonates. The agents according to the invention are preferably free of phosphate builders, i.e., they contain less than 1% by weight, preferably no deliberately added phosphate builder. The agents may also contain water-insoluble builders. Crystalline or amorphous water-dispersible alkali aluminosilicates are used as water-insoluble inorganic builder materials, in particular in amounts of up to 50% by weight, preferably not more than 40% by weight, in particular from 3 to 20% by weight, and particularly preferably from 1 to 15% by weight. Among these, crystalline sodium aluminosilicates in detergent quality, in particular zeolite A, zeolite P, zeolite MAP, and optionally zeolite X, 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), is preferred. Amounts close to the stated upper limit are preferably used in solid, particulate agents. Suitable aluminosilicates, in particular, have no particles with a grain size exceeding 30 µm and preferably consist of at least 80% by weight of particles with a size below 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. 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 agents according to the invention is preferably 0.1 to 20% by weight, preferably 1.0 to 15% by weight, and more preferably 2.0 to 12% by weight.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, these are present in amounts of preferably up to 50% by weight, in particular from 5 to 30% by weight, more preferably from 0.1 to 20% by weight. Compounds which, under perhydrolysis conditions, produce aliphatic peroxocarboxylic acids having preferably 1 to 10 C atoms, in particular 2 to 4 C atoms, and / or optionally substituted perbenzoic acid, can be used as bleach activators in the agents. Suitable substances are those which carry O- and / or N-acyl groups of the stated number of C 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 or LOBS), 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 respectively.the mixtures thereof described (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 a quaternized nitrogen atom, and / or oxygen-transferring sulfonimines and / or acylhydrazones. The hydrophilically substituted acyl acetals and the acyl lactams are also preferably used. Combinations of conventional bleach activators can also be used. Such bleach activators can, in particular in the presence of the above-mentioned hydrogen peroxide-providing bleaching agents, be used in the usual quantity range, preferably in amounts of 0.5 to 10 wt.%, in particular 1 to 8 wt.-%, based on the total product, but are preferably completely absent when percarboxylic acid is used as the sole bleaching agent. In addition to the conventional bleach activators, or instead of them, solid products may also contain sulfonimines and / or bleach-enhancing transition metal salts or transition metal complexes as so-called bleach catalysts. 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.The 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. 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 agent, further soil-release agents, preferably SRP polymers, although this embodiment is not preferred. These agents 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 or their derivatives with monomeric and / or polymeric diols known from the prior art, in particular polymers of ethylene terephthalates and / or polyethylene glycol terephthalates or anionically and / or non-ionically modified derivatives thereof. These are commercially available, for example, under the trade name Texcare®. Typical soil release polymers for polyester-containing textiles can be based, for example, on copolymers of polyester and polyether, including terephthalate, e.g., polypropylene terephthalate. Examples of commercially available soil release polymers include, for example,the polymers marketed 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 marketed by BASF under the trade name Sokalan, such as Sokalan SR 100, the polymers marketed by Sasol under the trade name Marloquest SL, the polymers marketed 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. Derivatives of diaminostilbene disulfonic acid or its alkali metal salts can be used as optical brighteners, particularly for textiles made from cellulose fibers (e.g. cotton). Suitable examples 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. Furthermore, brighteners of the substituted 4,4'-distyryldiphenyl type may be present, e.g., 4,4'-bis(4-chloro-3-sulfostyryl)diphenyl. 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 content of optical brighteners or brightener mixtures in the composition generally does not exceed 1% by weight, preferably 0.05 to 0.5% by weight. In a preferred embodiment of the invention, the composition is free of such active ingredients. Common foam regulators that can be used in the compositions according to the invention include, for example:Polysiloxane-silica mixtures, wherein the finely divided silica contained therein is preferably silanized or otherwise hydrophobized. The polysiloxanes can consist of linear compounds as well as crosslinked polysiloxane resins, as well as 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 is preferred. 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.%. 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 not more than 10 wt.%, in particular from 0.5 to 6 wt.%, particularly preferably from 0.3 to 2 wt.%. The agents according to the invention can 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 are 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 inventive compositions 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 in stabilizing the compositions is glycerol and 1,2-propylene glycol. Liquid compositions preferably comprise at least one polyol, preferably from the group consisting of glycerol and 1,2-propylene glycol, based on the total weight of the composition, preferably 0.1 to 10 wt.%, preferably 0.2 to 8.0 wt.%, and more preferably 0.5 to 5.0 wt.%. Other preferred organic solvents are organic amines and alkanolamines. The compositions 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. Agents according to the invention can contain enzymes in a concentration appropriate for the effectiveness of the agent. Preferably, all enzymes capable of catalytic activity in the agent according to the invention can be used, in particular protease, lipase, amylase, cellulase, hemicellulase, mannanase, tannase, xylanase, xanthanase, xyloglucanase, ß-glucosidase, pectinase, carrageenase, perhydrolase, oxidase, oxidoreductase, and mixtures thereof. Enzymes are advantageously present in the agent in an amount of 1 x 10 -8 to 5 wt.% based on active protein. Increasingly preferably, each enzyme is present in an amount of 1 x 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. Examples of proteases are subtilisins BPN' from Bacillus amyloliquefaciens and Carlsberg from Bacillus licheniformis, protease PB92, subtilisins 147 and 309, 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 under the trade names Esperase® and Savinase® by Novozymes, 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, for example, those sold under the trade names Durazym®, Relase®, Everlase®, Nafizym®, Natalase®, Kannase®, Progress Uno 101L® and Ovozyme® by Novozymes, those sold under the trade names Purafect®, Purafect® OxP, Purafect® Prime, Excellase®, Properase®, Preferenz P100® and Preferenz P300® by Danisco / DuPont, those sold under the trade name Lavergy pro 104 LS® by BASF, those sold under the trade name Protosol® by Advanced Biochemicals Ltd., which is sold under the trade name Wuxi® by Wuxi Snyder Bioproducts Ltd., which is sold under the trade names Proleather® and Protease P® by 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. Examples of amylases are the ^-amylases from Bacillus licheniformis, Bacillus amyloliquefaciens or Bacillus stearothermophilus and in particular also their further developments improved 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 development products of this ^-amylase are available under the trade names Duramyl® and Termamyl® ultra (both from Novozymes), Purastar® OxAm (Danisco / DuPont) and Keistase® (Daiwa Seiko Inc.).The ^-amylase from Bacillus amyloliquefaciens is marketed by Novozymes under the name BAN®, and derivatives of the ^-amylase from Bacillus stearothermophilus are marketed under the names BSG® and Novamyl®, also by Novozymes. Other suitable enzymes for this purpose are the ^-amylase from Bacillus sp. A 7-7 (DSM 12368) and the cyclodextrin glucanotransferase (CGTase) from Bacillus agaradherens (DSM 9948). Fusion products of all of the above molecules can also be used. Furthermore, the further developments of the ^-amylase from Aspergillus niger and A. oryzae, available from Novozymes under the trade name Fungamyl®, 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. TM 12L or Amplify Prime TM100L, the latter also from Novozymes, as well as the PREFERENZ S® series from Danisco / DuPont, including, for example, PREFERENZ S100®, PREFERENZ S1000® or PREFERENZ S210®. Variants of these enzymes obtainable by point mutations can also be used according to the invention. Suitable cellulases include those of bacterial or fungal origin. Chemically modified or protein-engineered mutants are included. Suitable cellulases are cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, e.g. Examples include 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 the alkaline or neutral cellulases with color-preserving 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 with 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 include a GH44 xyloglucanase, e.g., a xyloglucanase enzyme with 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. TM, Carezyme TM , Carezyme Premium TM , Celluclean TM (z.B. Celluclean TM 5000L ans Cellulclean TM 4000T), Celluclean Classic TM , Cellusoft TM , Endolase®, Renozyme® und Whitezyme TM (Novozymes A / S), Clazinase TM und Puradax HA TM (Genencor International Inc.), KAC-500(B) TM (Kao Corporation), Revitalenz TM 1000, Revitalenz TM 2000 und Revitalenz TM3000 (DuPont), as well as Ecostone® and Biotouch® (AB Enzymes). Suitable lipases include those 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 which are 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. TM , Lipex TM , Lipolex TM and Lipoclean TM(Novozymes A / S), Lumafast (Genencor / DuPont) and Lipomax (Gist-Brocades). Suitable mannanases are, for example, the Bacillus subtilis endo-^-mannanase, Bacillus sp. I633 Endo-^-mannanase, Bacillus sp. AAI12 Endo-^-mannanase, Bacillus sp. AA349 Endo-^-mannanase, Bacillus agaradhaerens NCIMB 40482 Endo-^-mannanase, Bacillus halodurans Endo-^-mannanase, Bacillus clausii Endo-^-mannanase, Bacillus licheniformis Endo-^-mannanase, Humicola insolens Endo-^-mannanase and Caldocellulosiruptor sp. Endo- ^-Mannanase (cf. e.g. US 6060299, WO 99 / 64573, US 6566114 and WO 99 / 64619). 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 are also those sold under the trade names Gamanase®, Pektinex AR®, X-Pect® or Pectaway® by 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 the enzymes and enzyme preparations available under the trade name Pyrolase® from Diversa Corp. In the cleaning agents described herein, the enzymes to be used can also be formulated together with accompanying substances, for example, from fermentation. In liquid formulations, the enzymes are preferably used as enzyme liquid formulation(s). Furthermore, it is possible to formulate two or more enzymes together so that a single granulate exhibits multiple enzyme activities. The enzymes can also be incorporated into water-soluble films, such as those used, for example, in the formulation of unit-dose detergents and cleaning agents. Such a film enables the release of the enzymes upon contact with water. As used herein, "water-soluble" refers to a film structurewhich is preferably completely water-soluble. Such a film preferably consists of (fully or partially hydrolyzed) polyvinyl alcohol (PVA). 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 several inhibitors / stabilizers are present, these figures refer to the total concentration. These can in particular be selected 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,specific peptide compounds and combinations thereof. 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. Further suitable additives for agents according to the invention can be selected, for example, from 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. In a preferred embodiment, the agent according to the invention comprises the at least one additive in an amount of 0,0.01 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 in addition to the agent. The agent 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 produce 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 of detergent or cleaning agent production. In a preferred embodiment, the agent contains one or more fragrances in an amount of typically up to 15% by weight, preferably 0.01 to 5% by weight, in particular 0.3 to 3% by weight, based on the total weight of the agent. 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 multi-phase agents. Suitable hydrophobic components are, for example, dialkyl ethers with identical 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.%. 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, are, for example, alkali metal and alkaline earth metal halides, in particular chlorides, and sulfates and nitrates, in particular sodium and potassium chloride and sulfate, and also ammonium chloride and sulfate or mixtures thereof. Such salts, as strong electrolytes which increase the ionic strength, support phase separation through the salt effect. Sodium chloride has proven particularly effective in this regard, whereas 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 wt.%, preferably 0.1 to 20 wt.%, e.g. 1 to 15 wt.-% or 1 to 5 wt.%. To adjust the viscosity, the washing or cleaning agent may contain one or more thickeners, preferably in an amount of 0.01 to 5 wt.%, more preferably 0.05 to 2.5 wt.%, even more preferably 0.1 to 1 wt.%. Suitable thickeners include, for example, organic natural thickeners (agar-agar, carrageenan, tragacanth, gum arabic, alginates, pectins, polyoses, guar gum, 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). 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.The following acrylic acid copolymers also fall under this category: (i) copolymers of two or more monomers from the group of acrylic acid, methacrylic acid and their simple esters, preferably formed with C1-4 alkanols (INCI Acrylates Copolymer), which include, for example, 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) crosslinked high molecular weight acrylic acid copolymers, which include, for example, the copolymers of C10-30 alkyl acrylates crosslinked with an allyl ether of pentaerythritol with one or more monomers from the group of acrylic acid, methacrylic acid and their simple esters, preferably formed with C. 1-4 -alkanols formed, esters (INCI Acrylates / C 10-30Alkyl Acrylate Crosspolymer). In addition to the thickening effect, these compounds can have further effects in detergents, such as graying protection. 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. Preferred thickeners are polysaccharides and heteropolysaccharides, in particular polysaccharide gums, e.g. gum arabic, agar, alginates, carrageens and their salts, guar, guaran, tragacanth, gellan, ramsan, dextran or xanthan and their derivatives, e.g. propoxylated guar, and their mixtures. 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. In general, their weight-average molecular weight is <250000 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 6g / mol is produced. 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-Types® / 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).Exemplary washing and cleaning agent compositions and suitable ingredients are described, for example, in WO 2001 / 44433 A1 or WO 2016 / 091650 A1. An exemplary composition of a washing agent according to the invention, in particular a liquid washing agent, comprises, in addition to the peptides and / or peptide conjugates described herein, the following components: water; and surfactants, in particular anionic and / or nonionic 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.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 For the purposes of the invention, cleaning performance is understood to mean the ability of an agent to partially or completely remove existing soiling, in particular the brightening performance of one or more soils on textiles. The cleaning performance is preferably determined as stated further below. Wash liquor is understood to be the use solution containing the washing agent which acts on the textiles or fabrics and thus comes into contact with the soils present on the textiles or fabrics.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 other suitable container. The cleaning performance can be determined in a washing system containing a detergent at a dosage of between 2.0 and 8.0 grams per liter of wash liquor and the peptides to be tested. A liquid reference detergent for such a washing system can, for example, have the following composition (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, more preferably between pH 8 and pH 9. The cleaning performance is determined by measuring the degree of cleaning of the washed textiles against soiling on textiles. For example, the washing process can take place 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). The degree of whiteness, ieThe lightening of the soiling, as a measure of the cleaning performance, is determined using optical measuring methods, preferably photometrically. A suitable device for this purpose is, for example, the Minolta CM508d spectrometer. The devices used for the measurement are usually calibrated beforehand with a white standard, preferably a supplied white standard. 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. Methods and uses A further subject 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.In various embodiments, the method 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 a low wash temperature, while 40°C is the preferred / average wash temperature in Europe. This includes both manual and mechanical methods, with mechanical methods being preferred due to their more precise controllability, for example with regard to the amounts used and contact times. Methods for cleaning textiles are generally characterized in that various cleaning-active substances are applied to the item to be cleaned in several process steps and are washed off after the contact time, or that the item to be cleaned is treated in some other way with a detergent or a solution or dilution of this agent.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 active ingredient. 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 liquor, 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 method according to the invention is carried out in the interior of a commercially available dishwasher.The cleaning program for a dishwasher 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 method according to the invention comprises at least a pre-wash cycle and a cleaning cycle. According to the invention, cleaning programs that include further cleaning or rinsing cycles, e.g., a final rinse cycle, are preferred. The method according to the invention is particularly preferably a component of a cleaning program comprising a pre-wash 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 the temperature of the cleaning liquor rises to values ​​above 30°C, preferably above 40°C, and in particular above 50°C. Alternative embodiments of this subject matter of the invention also include methods 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, methods for textile raw materials, fibers, or textiles with natural components are preferred, and very particularly for those with wool or silk.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 from about 20°C to about 60°C, particularly preferably about 20°C to about 40°C. 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 to improve the cleaning performance of the washing or cleaning agent on fatty and / or oily soils, preferably in a temperature range from about 20°C to about 60°C, particularly preferably about 20°C to about 40°C. A further subject matter 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 having the following amino acid sequence: (C). m X1X2X3(X4)<h2 style=";text-align:left;direction:ltr"> n <h2 style=";text-align:left;direction:ltr"> X5(C)<h2 style=";text-align:left;direction:ltr"> 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, where 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 listed in SEQ ID NO:1-27, wherein the peptide is preferably a textile-binding peptide. 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 having the following amino acid sequence: (C) m X1X2X3(X4) n X5(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 is independently 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 which has an amino acid sequence which is 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,has 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, more preferably k = 30-75, more preferably k = 40-60, most 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,is very particularly preferred. 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 brings about 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. The adhering peptides and / or peptide conjugates, in particular, realize the soil-repellent effect of the peptides and / or peptide conjugates after several wash cycles,Because the adhering peptides and / or peptide conjugates make it less easy for dirt to settle on or between the fibers. All facts, objects, and embodiments described for the agent according to the invention are also applicable to these inventions. 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.

[0002] EXAMPLES Example 1: Peptide sequences 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-RALRALQALEALEAL-GGGGS-(PEG) 43 4 NGLLIPQFLVAS-GGGGS-RSIVTFSLRQNR-GGGGS- 44 NGLLIPQFLVAS 5 NGLLIPQFLVAS-GGGGS-RALQALRALQALEAL-GGGGS- 45 NGLLIPQFLVAS 6 NGLLIPQFLVAS-GGGGS-RALRALQALEEALEAL-GGGGS- 46 NGLLIPQFLVAS 7 RSIVTFSLRQNR 25 8 RALQALRALQALEAL 1 9 RALRALQALEALEAL 5 10 NGLLIPQFLVAS 28 11 GGGGS 29 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.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). Peptides 7 to 9 are textile-binding peptides. Peptide 10 is a textile-nonbinding peptide. Peptide 11 is a peptide linker. Example 2: Adhesion test of peptides on polyester and blended fabrics. The adhesion of peptides 7 to 10 according to Table 1 to polyester fabric (WFK 30A, 100% polyester) and cotton / polyester blended fabric (WFK 20A, 50% cotton / 50% polyester) was tested. Test setup: Measurement method using fluorescamine in a 48-well microtiter plate with cloth pads with a diameter of 10 mm. Three pads 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.) was added. It 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. Immediately afterwards, the fluorescence was measured (absorbance 340 nm, emission 465 nm). 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 does not exhibit fluorescence without derivatization, the more fluorescamine-peptide conjugates present in the supernatant, the higher the fluorescence. The measured fluorescence values ​​were converted into adhesion in % as follows: (BA) / A, where B is the measured value for the test sample and A is the measured value for the blank.Table 2 shows what percentage of the applied amount (100%) of peptide adheres to the respective textile. The higher the value, the higher the binding affinity. Table 2: Adhesion of peptides to test fabric 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% Peptides 7 to 9 exhibit high binding affinity, thus they are textile-binding peptides. Peptide 10 exhibits no binding affinity, thus it is a textile-nonbinding peptide. Example 3: Washing test 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 % by weight of active ingredient % by weight of active ingredient in the raw material in the formulation Demineralized water.100 ad 100 Defoamers 100 <1% Citric acid 100 1-5% FAEOS 70 3-8% FAEO 100 2-11% LAS 96 3-20% C. 12 -C 18Fatty acid Na 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: Test batches ABCDEFG 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 min Dosage 3.1 g / l Washing volume 200 ml rotation, 40 rpm, fabric WFK 30A, WFK 20A, soiling: 25 µl engine oil, repetitions: 3. The textile fabrics were pre-washed, rinsed, and dried three times with 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 fabrics were then washed with the respective detergent formulation under test, 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 ABCDEFG 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 The peptides according to the invention lead to a whitening performance that is comparable to the reference sample (A) (peptides 1, 3) or even better (peptides 2, 4, 5, 6). In particular, peptides 4 and 5 show improved whitening performance on mixed fabrics. The improved whitening performance shows that the peptides not only contribute to the cleaning performance but also indicate a soil-repellent and / or soil-removing effect.

Claims

PATENT CLAIMS 1. Washing or cleaning agent, preferably 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 having the following amino acid sequence: (C)mX1X2X3(X4)nX5(C)o, wherein 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 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 any of the amino acid sequences recited 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, independently of one another, are 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 recited 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) contains no P and preferably also no G and even more preferably also no 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)nX5 comprises at least one sequence X6X7X8, wherein X6 is a charged or uncharged amino acid, preferably R, K, E or Q, and X7 and X8, independently of one another, are uncharged amino acids with the exception of P and G, preferably A, L, or M, even more preferably A or L, and / or (iii) (X4)n comprises 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). 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) nX5 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% 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.

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 the group consisting of (I) (GGGGS) nwith 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; consisting of, preferably the linker is a linker 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 one of the amino acid sequences mentioned 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 having the following amino acid sequence: (C). m X1X2X3(X4) n X5(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 any of the amino acid sequences listed in SEQ ID NO: 1-27, where s = 1; where Z1 and Z7 independently of one another are -(C2H4O) kare, where k = 5-100, p and w are 0 or 1 and p+w = 0 to 2; where 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, where q and v are 0 or 1 and q+v = 0 to 2; where Z3 and Z5 are linkers, preferably peptide linkers, where 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 particularly preferably 4.

11. A washing or cleaning agent, preferably a textile detergent, comprising at least one peptide conjugate according to claim 10. 12.A method for cleaning textiles and / or hard surfaces, in particular dishes, characterized in that a washing or cleaning agent according to one of claims 1 to 9 or 11 is used in at least one method step, wherein the method is preferably carried out in a temperature range from 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 from 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 agent, 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 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.

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