Sayeed Sadulla

Green chemistry approaches to leather tanning process for making chrome-free leather by unnatural amino acids

In the present study, green and sustainable method or eco-friendly approaches to tanning process based on unnatural D-amino acids (D-AA)-aldehyde (Ald) as a substitute for chrome-free tanning has been attempted. The distribution of optically active D-AA in tanned leather, the hydrothermal stability, the mechanical properties and resistance to collagenolytic activity of tanned leather, the evaluation of eco-friendly characteristics were investigated. Scanning electron microscopic (SEM) and Atomic force microscopic (AFM) analyses indicate the surface morphology and roughness, respectively, of the tanned leather collagen matrix. Shrinkage and Differential scanning calorimetric (DSC) analyses shows that the shrinkage temperature (T(s)) and denaturation temperature (T(d)) of tanned leather are related to the content of D-AA+Ald present in the leather matrix. It has been found that the T(s) of D-AA tanned leather is more than that of Ald tanned leather and also more or less equal to chrome tanned leather. Environmental impact assessment (EIA) shows that the developed process results in significant reduction in total solids content (TSC) and improves better biodegradability of organic compound present in the effluent compared to chrome tanning.

Experimental and theoretical studies on Gallic acid assisted EDC/NHS initiated crosslinked collagen scaffolds.

The effect of Gallic acid (GA) in the presence of 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC)/N-hydroxysuccinimide (NHS) on collagen scaffold is investigated. The thermal mechanical analyzer (TMA), differential scanning calorimetric (DSC), and thermogravimetric analysis (TGA) including tensile strength (TS, 180 ± 3 MPa), denaturation temperature (Td, 80.03°C), % elongation (% E, 180 ± 9) and weight loss (31.76%), indicate that the modification improves the structural integrity and stability of the collagen scaffold. The GA-EDC/NHS treatment inhibits the action of collagenase against collagen degradation compared to GA and EDC/NHS. It is concluded from docking studies that GA binds with collagen like peptide (CLP) and collagenase through multiple H-bonds and hydrophobic interactions leading to low binding energy -5.1 and -5.3 Kcal/mol, respectively. The hydrophobic core of the GA molecules, probably incorporates itself into the hydrophobic areas of the collagen groups, whereas OH and COOH moieties of GA establish multiple H-bonds with neighboring collagen molecules and carboxamide bond, thereby improving the swelling and water uptake properties, biocompatibility and cell adhesion properties. This results in improving stability of the scaffold, which prevents the free access of the collagenase to reactive sites in the triple helical collagen chains.

Novel collagen scaffolds prepared by using unnatural D-amino acids assisted EDC/NHS crosslinking

This work discusses the preparation and characterization of novel collagen scaffolds by using unnatural D-amino acids (Coll-D-AAs)-assisted 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC)/N-hydroxyl succinimide(NHS)-initiated crosslinking. The mechanical strength, hydrothermal and structural stability, resistance to biodegradation and the biocompatibility of Coll-D-AAs matrices were investigated. The results from Thermo mechanical analysis, Differential scanning calorimetric analysis and Thermo gravimetric analysis of the Coll-D-AAs matrices indicate a significant increase in the tensile strength (TS, 180 ± 3), % elongation (% E, 80 ± 9), elastic modulus (E, 170 ± 4) denaturation temperature (T d, 108 ± 4) and a significant decrease in decomposition rate (T g, 64 ± 6). Scanning electron microscopic and Atomic force microscopic analyses revealed a well-ordered with properly oriented and well-aligned structure of the Coll-D-AAs matrices. FT-IR results suggest that the incorporation of D-AAs favours the molecular stability of collagen matrix. The D-AAs stabilizing the collagen matrices against degradation by collagenase would have been brought about by protecting the active sites in collagen. The Coll-D-AAs matrices have good biocompatibility when compared with native collagen matrix. Molecular docking studies also indicate better understanding of bonding pattern of collagen with D-AAs. These Coll-D-AAs matrices have been produced in high mechanical strength, thermally and biologically stable, and highly biocompatible forms that can be further manipulated into the functional matrix suitable in designing scaffolds for tissue engineering and regenerative medical applications.

Development of D-lysine-assisted 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide/N-hydroxysuccinimide-initiated cross linking of collagen matrix for design of scaffold†

This work discusses the preparation and characterization of collagen scaffold with presence of D-Lysine (Coll-D-Lys)-assisted 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC)/N-hydroxysuccinimide (NHS)-initiated cross linking. The mechanical strength, thermal and structural stability, resistance to biodegradation and cell viability of this scaffold was investigated. The results of the Coll-D-Lys-EDC/NHS scaffold also indicate an increase in the tensile strength (T(S)), percentage of elongation (% E), denaturation temperature (T(d)), and decrease the decomposition rate. Scanning electron microscopic (SEM) and atomic force microscopic (AFM) analyses revealed a well ordered with properly oriented and well-aligned structure of scaffold. The D-Lys stabilizes the scaffold against degradation by collagenase than L-Lys. The cell assay showed more than 98 ± 2% fibroblast viability (NIH 3T3) after 72 h of culture Coll-D-Lys-scaffold when compared with native Coll and Coll-L-Lys-scaffold. The proteolytic machinery is not well equipped to deal with Coll-D-Lys-scaffold than Coll-L-Lys-scaffold. Incorporating D-Lys in scaffold design has the potential to improve existing collagen stability and create new topologies inaccessible to homochiral molecules. This method may assist in the functionalization of the scaffold for regenerative applications.

Studies on collagen-tannic acid-collagenase ternary system: inhibition of collagenase against collagenolytic degradation of extracellular matrix component of collagen

We report the detailed studies on the inhibitory effect of tannic acid (TA) on Clostridium histolyticum collagenase (ChC) activity against degradation of extracellular matrix component of collagen. The TA treated collagen exhibited 64% resistance against collagenolytic hydrolysis by ChC, whereas direct interaction of TA with ChC exhibited 99% inhibition against degradation of collagen and the inhibition was found to be concentration dependant. The kinetic inhibition of ChC has been deduced from the extent of hydrolysis of N-[3-(2-furyl) acryloyl]-Leu-Gly-Pro-Ala (FALGPA). This data provides a selective competitive mode of inhibition on ChC activity seems to be influenced strongly by the nature and structure of TA. TA showed inhibitor activity against the ChC by molecular docking method. This result demonstrated that TA containing digalloyl radical possess the ability to inhibit the ChC. The inhibition of ChC in gaining new insight into the mechanism of stabilization of collagen by TA is discussed.

Collagen Coated Nanoliposome as a Targeted and Controlled Drug Delivery System

The collagen coated nanoliposome (CCNL) have been prepared and characterized in order to develop a targeted and controlled drug delivery system. The zeta potential (ZP) measurement, Fourier transform infrared (FT‐IR) spectral and Scanning Electron Microscopy (SEM) and Cell viability assay data showed that the collagen coated nanoliposome particle size and charges, structural interaction and surface morphology and high bio‐cyto‐compatibility of collagen coated nanoliposome. The particle sizes of nanoliposome (NL) and collagen coated nanoliposome are 20–300 nm and 0.1–10 μm respectively. The introduction of triple helical, coiled coil and fibrous protein of collagen into nanoliposome can improves the stability of nanoliposome, resistant to phospholipase activities and decreasing the phagocytosis of liposomes by reticuloendothelial system. The collagen coated nanoliposome is expected to be used as for targeted and controlled drug delivery system, and tissue engineering application.