Does L to D-amino acid substitution trigger helix→sheet conformations in collagen like peptides adsorbed to surfaces?

Punitha Velmurugan; Raghava Rao Jonnalagadda; Kamatchi Sankaranarayanan; Aruna Dhathathreyan

doi:10.1016/j.msec.2015.07.057

Does L to D-amino acid substitution trigger helix→sheet conformations in collagen like peptides adsorbed to surfaces?

Mater Sci Eng C Mater Biol Appl. 2015 Dec 1:57:249-56. doi: 10.1016/j.msec.2015.07.057. Epub 2015 Aug 1.

Authors

Punitha Velmurugan¹, Raghava Rao Jonnalagadda², Kamatchi Sankaranarayanan³, Aruna Dhathathreyan⁴

Affiliations

¹ Council of Scientific and Industrial Research-Central Leather Research Institute, Chemical Laboratory, Adyar, Chennai 600 020, India; University of Madras, Centre for Advanced Study in Crystallography and Biophysics, Guindy Campus, Chennai 600 025, India.
² Council of Scientific and Industrial Research-Central Leather Research Institute, Chemical Laboratory, Adyar, Chennai 600 020, India. Electronic address: jrrao@clri.res.in.
³ Council of Scientific and Industrial Research-Central Leather Research Institute, Chemical Laboratory, Adyar, Chennai 600 020, India.
⁴ Council of Scientific and Industrial Research-Central Leather Research Institute, Biophysics Laboratory, Adyar, Chennai 600 020, India.

PMID: 26354261
DOI: 10.1016/j.msec.2015.07.057

Abstract

The present work reports on the structural order, self assembling behaviour and the role in adsorption to hydrophilic or hydrophobic solid surfaces of modified sequence from the triple helical peptide model of the collagenase cleavage site in type I collagen (Uniprot accession number P02452 residues from 935 to 970) using (D)Ala and (D)Ile substitutions as given in the models below: Model-1: GSOGADGPAGAOGTOGPQGIAGQRGVV GLOGQRGER. Model-2: GSOGADGP(D)AGAOGTOGPQGIAGQRGVVGLOGQRGER. Model-3: GSOGADGPAGAOGTOGPQG(D)IAGQRGVVGLOGQRGER. Collagenase is an important enzyme that plays an important role in degrading collagen in wound healing, cancer metastasis and even in embryonic development. However, the mechanism by which this degradation occurs is not completely understood. Our results show that adsorption of the peptides to the solid surfaces, specifically hydrophobic triggers a helix to beta transition with order increasing in peptide models 2 and 3. This restricts the collagenolytic behaviour of collagenase and may find application in design of peptides and peptidomimetics for enzyme-substrate interaction, specifically with reference to collagen and other extra cellular matrix proteins.

Keywords: Adsorption; Chirality; Collagen like peptide; Dichroism; d-amino acid.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Adsorption
Amino Acid Sequence
Amino Acid Substitution*
Binding Sites
Collagen / chemistry*
Collagen / ultrastructure*
Collagenases / chemistry*
Crystallization / methods
Hydrophobic and Hydrophilic Interactions
Isomerism
Molecular Sequence Data
Peptides / chemistry*
Protein Binding
Protein Conformation
Structure-Activity Relationship
Surface Properties

Substances

Peptides
Collagen
Collagenases