Does L to D-amino acid substitution trigger helix→sheet conformations in collagen like peptides adsorbed to surfaces?
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.
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.
Punitha
P
Velmurugan
Council of Scientific and Industrial Research-Central Leather Research Institute, Chemical Laboratory, Adyar, Chennai 600 020, India. Electronic address: jrrao@clri.res.in.
Raghava Rao
RR
Jonnalagadda
Council of Scientific and Industrial Research-Central Leather Research Institute, Chemical Laboratory, Adyar, Chennai 600 020, India.
Kamatchi
K
Sankaranarayanan
Council of Scientific and Industrial Research-Central Leather Research Institute, Biophysics Laboratory, Adyar, Chennai 600 020, India.
Aruna
A
Dhathathreyan
D000327:Adsorption; D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D001665:Binding Sites; D003094:Collagen / Q000737:chemistry* / Q000648:ultrastructure*; D017364:Collagenases / Q000737:chemistry*; D003460:Crystallization / Q000379:methods; D057927:Hydrophobic and Hydrophilic Interactions; D007536:Isomerism; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013499:Surface Properties
D010455:Peptides; D003094:Collagen; D017364:Collagenases
Adsorption; Chirality; Collagen like peptide; Dichroism; d-amino acid