Stabilization of type I collagen against collagenases (type I) and thermal degradation using iron complex

Structure and dynamics of water in native and tanned collagen fibers: Effect of crosslinking

“…In the present study, collagen has been interacted with a series of small molecules bearing flavonoid structure, formaldehyde and a mixture of 15 molecular species of Cr(III) salts contained in basic chromium sulfate [10]. The interactions of different molecules like flavonoids, formaldehyde or Cr(III) species contained in basic chromium sulfate are known to induce inter-and intramolecular crosslinking and long range ordering in collagen fibers [8][9][10]. The effect of ligand interactions on the hydration structure and dynamics of collagen has been studied in this present work.…”

“…The effect of crosslinking in collagen on the functional properties of skin has attracted wide attention in view of the significance in understanding tanning phenomena [5,6] as well as management of skin disorders [7]. It is now established that treatment of collagen fibers with metal salts as well as polyphenolic substances derived from plant materials could alter the tertiary and quaternary structures of collagen leading to changes in the stability of the protein against degradation by collagenases and thermo mechanical stress [8,9]. Changes in the long range ordering of collagen as observed through alterations of the D periodicity in the quaternary structure of collagen fibers attributed to crosslinking have been reported [10].…”

Laboratory assessment of tetrakis(hydroxymethyl)phosphonium sulfate as dissolver for scales formed in sour gas wells

“…It can be degraded in both aerobic and anaerobic environments through hydrolysis, oxidation, biological and photo reactions [10]. The degradation reactions are affected by many factors such as temperature, pH value, O 2 level, light, microbes and the presence of mild steel [10,11]. The breakdown products include trishydroxymethylphosphine oxide (THPO), bishydroxymethyl phosphonic acid (BMPA), and possibly a formaldehyde adduct of trihydroxy compound [12].…”

Effect of surfactants on the thermal, conformational and rheological properties of collagen

“…No such change has been observed hence, the surfactants used in this study do not bring about denaturation of collagen at the concentrations used in this study. The Rpn ratio (ratio of positive to negative peak in a CD spectrum) [15] given in Table 1 indicates that collagen is folded or precipitated at an extreme surfactants concentration.…”