Investigation on interaction of tannic acid with type I collagen and its effect on thermal, enzymatic, and conformational stability for tissue engineering applications

Abstract

Collagen is an essential component of tissues, which is the most abundant component in extracellular matrix and highly conserved across the animal kingdom. It can assemble into fiber and play an essential role in cell adhesion and growth and could be extremely useful in tissue engineering. In this study, the effect of tannic acid (TA) on the thermal, enzymatic and conformational stability of type I collagen has been investigated for the development of collagen-based biomaterials. Interaction of TA with collagen demonstrates the role of hydrogen bonding and hydrophobic interaction in providing the thermal and enzymatic stability. Thermal analysis studies reveal that, hydrothermal stability of collagen increases as well as inhibits the breakdown of collagenase by formation of hydrogen bonds and hydrophobic interactions. TA binds to the collagen with high affinity because the structural flexibility of the collagen compensates for the structural rigidity of the phenolics. Increase in concentration of TA induces significant change in the conformation of triple helix. The free binding energy of TA with collagen-like peptide was determined to be in the range of -9.4 to -11.2 kcal mol(-1), which was calculated by using Autodock Vina software and showed numerous hydrophobic and hydrogen bond interactions. We anticipate that these collagen-based biomaterials hold great potential for biomedical applications.

Controlled release of methylene blue from glutaraldehyde‐modified gelatin

“…The crosslinking agents can react with the functional groups of gelatin (e.g., –COOH, –NH 2 , –OH, and –CONH–) and form the intramolecular and/or intermolecular gelatin crosspolymers to change the structure of gelatin as well as decrease the thermal and enzymatic degradability (Abd El‐Hady & Albishri, ). Commonly applied crosslinking agents include metal salts, organic acids, genipin, transglutaminase, and dialdehyde carboxymethyl cellulose (De Clercq et al, ; Kaewruang, Benjakul, Prodpran, Encarnacion, & Nalinanon, ; Li, Ye, Li, Li, & Mu, ; Velmurugan, Singam, Jonnalagadda, & Subramanian, ; Wang, Liu, Ye, Wang, & Li, ).…”

“…Commonly applied crosslinking agents include metal salts, organic acids, genipin, transglutaminase, and dialdehyde carboxymethyl cellulose. (De Clercq et al, 2016;Kaewruang, Benjakul, Prodpran, Encarnacion, & Nalinanon, 2014;Li, Ye, Li, Li, & Mu, 2016;Velmurugan, Singam, Jonnalagadda, & Subramanian, 2014;Wang, Liu, Ye, Wang, & Li, 2015).…”

Two-dimensional infrared spectroscopic study on the thermally induced structural changes of glutaraldehyde-crosslinked collagen

“…Nevertheless, this structural hierarchy is susceptible to the damage and denaturation caused by a number of factors including heat, enzyme, strong acids or alkali and heavy metals, among which the denaturation due to heat treatment is always encountered [7]. In general, the most commonly used method to improve the thermal stability of collagen is the introduction of exogenous crosslinking bonds due to its plentiful functional groups such as ACOOH, ANH 2 , AOH and ACONH [8].…”

Chitosan/collagen blends with inorganic and organic additive—A review

“…[134,135] Tannic acid was used for many decades in the treatment of burns. [136][137][138][139] In biomaterial science, it was studied as a collagen [140][141][142][143][144][145][146][147][148][149][150][151][152] and chitosan, [153][154][155][156][157][158][159][160] as well as their mixture [161] cross-linker. Tannic acid has antioxidant and antimicrobial properties.…”