G. Krishnamoorthy, R. Selvakumar, T. Sastry
Jun 15, 2013
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Influential Citations
16
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Journal
Biochemical Engineering Journal
Abstract
Abstract The effect of selected d -amino acids ( d -AAs) on collagen with 1-ethyl-3-(3-dimethylamino propyl)carbodiimide (EDC)/N-hydroxysuccinimide (NHS) initiated crosslinking is evaluated by using experimental and modelling tools. The experimental results suggest that d -Lysine ( d -Lys) plays a pivotal role in the self-assembly and conformation of collagen fibrils than d -Alanine ( d -Ala) and d -Glutamic acid ( d -Glu). The SDS-PAGE, absorption spectrum and viscosity measurements indicate significant differences in the d -Lys crosslinked collagen when compared to other systems. The CD spectra show an increase in the peak intensity at 220 nm in the presence of d -Lys, which could be due to increase in propensity of the structure to form a triple helix. Modelling studies indicated that d -Lys bind with collagen-like peptide (CLP) through multiple H-bonding and hydrophobic interactions. d -Lys has the lowest binding energy (−4.2 kcal/mol, indicating strongest interactions) when compared to d -Ala and d -Glu (−3.6 and −3.7 kcal/mol, respectively). Orientational changes in the collagenase on CLP- d -Lys are observed which may decrease its accessibility to degradation and stabilise CLP against the action of the former. d -Lys has the lowest binding energy and improved fibrillar-assembly and staggered alignment without the undesired structural stiffness and aggregations. The information derived from the present study could help in designing heterochiral collagen-based biomaterial.