25191-13-3 Usage
Description
Poly-L-proline, a synthetic polymer, is composed of repeated units of the amino acid proline. It is characterized by a unique helical structure that resembles the conformation of proline-rich regions in proteins. This feature, along with its biocompatibility and biodegradability, makes it a valuable tool in various fields, including the study of protein folding and stability, drug delivery, and tissue engineering.
Uses
Used in Biochemistry and Biotechnology:
Poly-L-proline is used as a model system for studying protein folding and stability due to its unique helical structure that mimics proline-rich regions in proteins.
Used in Drug Delivery Systems:
Poly-L-proline is used as a component in drug delivery systems to improve the delivery and efficacy of therapeutic agents, taking advantage of its biocompatibility and biodegradability.
Used in Tissue Engineering:
Poly-L-proline is used as a scaffold for tissue engineering, supporting the development of implants and tissue regeneration therapies, owing to its ability to mimic the natural extracellular matrix and promote cell attachment and growth.
Used in Peptide-based Drug Design:
Poly-L-proline is used in the design of peptide-based drugs, leveraging its structural properties to study protein-protein interactions and develop novel therapeutic agents.
Check Digit Verification of cas no
The CAS Registry Mumber 25191-13-3 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 2,5,1,9 and 1 respectively; the second part has 2 digits, 1 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 25191-13:
(7*2)+(6*5)+(5*1)+(4*9)+(3*1)+(2*1)+(1*3)=93
93 % 10 = 3
So 25191-13-3 is a valid CAS Registry Number.
InChI:InChI=1/C5H9NO2/c7-5(8)4-2-1-3-6-4/h4,6H,1-3H2,(H,7,8)
25191-13-3Relevant articles and documents
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Okuda
, p. 358 (1957)
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Mazelis,Fowden
, p. 801 (1969)
Babievskii,K.K. et al.
, (1965)
MODIFIED INTERLEUKIN-7 PROTEINS AND USES THEREOF
-
, (2021/10/22)
Provided are a modified IL-7 polypeptide and a fusion protein containing the modified IL-7 polypeptide. The fusion protein of the modified IL-7 includes: a first domain containing an interleukin-7 polypeptide; a second domain containing an oligopeptide having 1 to 10 amino acid residues (with proviso that the second domain excludes the oligopeptide consisting of methionine and/or glycine); and (c) a third domain which prolongs the half-life of the IL-7 fusion protein. The modified IL-7 polypeptide is composed of the (a) first domain and the (b) second domain. The modified IL-7 polypeptide and the fusion protein are expressed in a higher yield than the wild-type IL-7 and shows increased stability.
Direct monitoring of biocatalytic deacetylation of amino acid substrates by1H NMR reveals fine details of substrate specificity
De Cesare, Silvia,McKenna, Catherine A.,Mulholland, Nicholas,Murray, Lorna,Bella, Juraj,Campopiano, Dominic J.
supporting information, p. 4904 - 4909 (2021/06/16)
Amino acids are key synthetic building blocks that can be prepared in an enantiopure form by biocatalytic methods. We show that thel-selective ornithine deacetylase ArgE catalyses hydrolysis of a wide-range ofN-acyl-amino acid substrates. This activity was revealed by1H NMR spectroscopy that monitored the appearance of the well resolved signal of the acetate product. Furthermore, the assay was used to probe the subtle structural selectivity of the biocatalyst using a substrate that could adopt different rotameric conformations.
