Document Detail

Sequence recombination improves target specificity in a redesigned collagen peptide abc-type heterotrimer.
MedLine Citation:
PMID:  23042255     Owner:  NLM     Status:  MEDLINE    
Stability of the collagen triple helix is largely governed by its imino acid content, namely the occurrence of proline and 4R-hydroxyproline at the X and Y positions, respectively, of the periodic (Gly-X-Y)(n) sequence. Although other amino acids at these positions reduce stability of the triple helix, this can be partially compensated by introducing intermolecular side-chain salt bridges. This approach was previously used to design an abc-type heterotrimer composed of one basic, one acidic, and one neutral imino acid rich chain (Gauba and Hartgerink, J Am Chem Soc 2007;129:15034-15041). In this study, an abc-type heterotrimer was designed to be the most stable species using a sequence recombination strategy that preserved both the amino acid composition and the network of interchain salt bridges of the original design. The target heterotrimer had the highest T(m) of 50 °C, 7 °C greater than the next most stable species. Stability of the heterotrimer decreased with increasing ionic strength, consistent with the role of intermolecular salt bridges in promoting stability. Quantitative meta-analysis of these results and published stability measurements on closely related peptides was used to discriminate the contributions of backbone propensity and side-chain electrostatics to collagen stability.
Sumana Giddu; Fei Xu; Vikas Nanda
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2012-11-05
Journal Detail:
Title:  Proteins     Volume:  81     ISSN:  1097-0134     ISO Abbreviation:  Proteins     Publication Date:  2013 Mar 
Date Detail:
Created Date:  2013-01-28     Completed Date:  2013-08-02     Revised Date:  2014-03-09    
Medline Journal Info:
Nlm Unique ID:  8700181     Medline TA:  Proteins     Country:  United States    
Other Details:
Languages:  eng     Pagination:  386-93     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 Wiley Periodicals, Inc.
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MeSH Terms
Amino Acid Sequence
Chemistry Techniques, Synthetic / methods*
Circular Dichroism
Collagen / chemistry*
Models, Molecular
Osmolar Concentration
Protein Denaturation
Protein Folding
Protein Interaction Mapping / methods*
Protein Stability
Sodium Chloride / chemistry
Static Electricity
Grant Support
DP2 OD006478/OD/NIH HHS; DP2 OD006478-01/OD/NIH HHS
Reg. No./Substance:
7647-14-5/Sodium Chloride; 9007-34-5/Collagen

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