title: Stabilization of collagen through bioconversion: An insight in protein-protein interaction.
abstract: Collagen is a natural protein, which is used as a vital biomaterial in tissue engineering. The major concern about native collagen is lack of its thermal stability and weak resistance to proteolytic degradation. In this scenario, the crosslinking compounds used for stabilization of collagen are mostly of chemical nature and exhibit toxicity. The enzyme mediated crosslinking of collagen provides a novel alternative, nontoxic method for stabilization. In this study, aldehyde forming enzyme (AFE) is used in the bioconversion of hydroxylmethyl groups of collagen to formyl groups that results in the formation of peptidyl aldehyde. The resulted peptidyl aldehyde interacts with bipolar ions of basic amino acid residues of collagen. Further interaction leads to the formation of conjugated double bonds (aldol condensation involving the aldehyde group of peptidyl aldehyde) within the collagen. The enzyme modified collagen matrices have shown an increase in the denaturation temperature, when compared with native collagen. Enzyme modified collagen membranes exhibit resistance toward collagenolytic activity. Moreover, they exhibited a nontoxic nature. The catalytic activity of AFE on collagen as a substrate establishes an efficient modification, which enhances the structural stability of collagen. This finds new avenues in the context of protein-protein stabilization and discovers paramount application in tissue engineering.
authors.affiliation: CHORD, CSIR-Central Leather Research Institute, Council of Scientific and Industrial Research, Adyar, Chennai-600 020, India.
authors.forename: Nagarajan
authors.initials: N
authors.lastname: Usharani
authors.forename: Gladstone Christopher
authors.initials: GC
authors.lastname: Jayakumar
authors.forename: Swarna Vinodh
authors.initials: SV
authors.lastname: Kanth
authors.forename: Jonnalagadda Raghava
authors.initials: JR
authors.lastname: Rao
mesh_terms: D000429:Alcohol Oxidoreductases / Q000378:metabolism; D000447:Aldehydes / Q000032:analysis; D000596:Amino Acids / Q000378:metabolism; D000818:Animals; D002384:Catalysis; D002470:Cell Survival; D003094:Collagen / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D011485:Protein Binding; D055550:Protein Stability; D017208:Rats, Wistar; D012996:Solutions; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature; D013718:Tensile Strength; D014783:Viscosity
chemical_list: D000447:Aldehydes; D000596:Amino Acids; D012996:Solutions; D003094:Collagen; D000429:Alcohol Oxidoreductases
keywords: aldehyde forming enzyme; bioconversion; collagen; denaturation temperature; stabilization