A kind of leech polypeptide with antithrombotic and brain nerve cell protection and its application
A brain nerve cell, leech polypeptide technology, applied in extracellular fluid diseases, peptides, blood diseases, etc., can solve the problem of unclear active ingredients, and achieve the effect of improving neurobehavior, reducing brain edema, and being easy to prepare in large quantities.
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Embodiment 1
[0055] Example 1 Separation of polypeptide whitmantides A-C
[0056] (1) 3 kg of leeches were dried, washed, soaked, pulverized and homogenized with physiological saline, and the homogenate was freeze-thawed to obtain an extract. The obtained extract is processed by an ultrafiltration membrane with a molecular weight cut-off of 50KDa, and the ultrafiltrate part with a molecular weight of less than 50KDa is collected, and the obtained ultrafiltrate is subjected to solid-phase desalination, concentrated under reduced pressure or freeze-dried to obtain the total extract (13g) . Total extracts were separated by gel Sephadex G25 at 4-8°C. The ultra-high performance liquid chromatography-mass spectrometry (UPLC-MS) method was used for analysis, tracking and detection, and the fractions containing the peptide compounds were collected, concentrated under reduced pressure or vacuum dried to obtain a peptide-enriched site (10 g).
[0057] (2) Take the polypeptide enriched part in step...
Embodiment 2
[0061] Example 2 Structural characterization of the polypeptide whitmantide A
[0062] The polypeptide whitmantide A prepared in Example 1 is an amorphous powder, UV (H 2 O)λ max (logε): 195(3.20). IR(KBr)ν max :3275.5,2960.2,1657.52,1541.81cm -1 . HR-ESI-MS m / z 658.4155[M+H] + (calcd for C 30 H 56 N 7 O 9 :658.4140). The N-terminal sequencing of whitmantide A was performed by Edman degradation method, and the amino acid sequence was determined to be NH 2 -Leu-Leu-Ser-Gly-Val-Leu-Gly-COOH. The MS / MS secondary mass spectrum showed that the a, b and y ion fragments of this compound were consistent with its amino acid sequence, and the above results further verified the amino acid linking sequence of whitmantide A. The results of Marfey analysis showed that whitmantide A contained two D-leucines and one L-leucine, and other chiral amino acids were all L-shaped. The absolute configuration of whitmantide A was determined by solid-phase synthesis. The positions of D- an...
Embodiment 3
[0063] Example 3 Structural characterization of the polypeptide whitmantide B
[0064] The polypeptide whitmantide B prepared in Example 1 is an amorphous powder, UV (H 2 O)λ max (logε): 196(3.18). IR(KBr)ν max :3275.5,2957.3,1640.16,1544.7,1132.97cm -1 ;HR-ESI-MS m / z715.4331[M+H] + (calcd for C 32 H 59 N 8 O 10 :715.4354). The N-terminal sequencing of whitmantide B was performed by Edman degradation method, and the amino acid sequence was determined to be NH 2 -Leu-Leu-Ser-Gly-Val-Leu-Gly-Gly-COOH. MS / MS secondary mass spectrum showed that the a, b and y ion fragments of this compound were consistent with its amino acid sequence, and the above results further verified the amino acid linking sequence of whitmantide B. The results of Marfey analysis showed that whitmantide B contained two D-leucines and one L-leucine, and other chiral amino acids were all L-type. The absolute configuration of whitmantide B was determined by solid-phase synthesis. The positions of D-...
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