Evidence for the existence of hydrophobic interactions as a stabilizing factor in collagen structure

Schnell, Joachim

doi:10.1016/0003-9861(68)90254-3

Cited by 33 publications

(9 citation statements)

References 15 publications

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“…Perturbant structural and functional features such as linear hydrocarbon chain length, chain isomerism and position and number of potential hydrogen-bonding groups were found to constitute the main factors determining solvent effects on thermal stability and renaturation kinetics of collagen in solution (Russell & Cooper, 1969a,b, 1970Hart et al, 1971;Cooper et al, 1971). Similar solvent effects have been reported by other workers for soluble collagen (Herbage et al, 1968;Schnell, 1968;Harrap, 1969;Bianchi et al, 1970) and globular proteins (Schrier & Scheraga, 1962;Herskovits et al, 1970a,b,c;Kaminsky et al, 1972).…”

supporting

confidence: 72%

“…Evidence for direct solvent-protein interaction moderated by hydro-1973 carbon chain length, has been reported in studies of the binding of alcohol homologues to collagen membranes (Bianchi et al, 1970). The influence of hydrocarbon chain length on lyotropic activity has led previous workers to conclude that alcohols disrupt internal hydrophobic bonding in proteins generally (Kauzman, 1959;von Hippel & Wong, 1965;Herskovits et al, 1970a) and, by analogy, in soluble and insoluble collagens (Schnell & Zahn, 1965;Herbage et al, 1968;Schnell, 1968;Harrap, 1969). For collagen fibrils, the positive temperature, dependence of formation (Gross, 1958;Cooper, 1970;Cassel, 1971) is indicative of an endothermic, and hence entropy-driven, process, implicating solvent-labile hydrophobic interactions between apolar side chains in adjacent molecules in aggregation and stabilization.…”

Section: Alcohol Effects On Soluble Andprecipitated Collagensmentioning

confidence: 94%

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Effect of alcohols and neutral salt on the thermal stability of soluble and precipitated acid-soluble collagen

Russell

1973

Biochemical Journal

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The effects of mono- and poly-hydric alcohols in the presence of KCl on the intrinsic stability of collagen molecules in dilute acid solution were compared with corresponding solvent and salt effects on the increased stability of the aggregated molecules in salt-precipitated fibrils. Salt addition decreased solubility and increased the thermal stability of fibrils, but progressively decreased the stability of collagen molecules in solution. In contrast, the alcohols enhanced solubility and decreased fibril stability, the effects increasing with solvent hydrocarbon chain length and with decreasing hydroxyl/methylene-group ratio. Molar destabilization of dissolved collagen by alcohols was lower than for fibrils, and at low salt concentration, both ethylene glycol and glycerol were structural stabilizers. Electron-micrograph studies indicated that salt-precipitated fibrils tended to adopt the native aggregation mode, and qualitatively similar solvent effects were observed in insoluble collagens. Implications of the experimental findings are discussed in terms of a model in which electrostatic and apolar interactions mainly govern the excess of stability in collagen fibrils whereas intrinsic stability of single molecules is a function of polar interactions and polypeptide-chain rigidity.

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supporting

confidence: 72%

Section: Alcohol Effects On Soluble Andprecipitated Collagensmentioning

confidence: 94%

Effect of alcohols and neutral salt on the thermal stability of soluble and precipitated acid-soluble collagen

Russell

1973

Biochemical Journal

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“…As the aliphatic chain length of the denaturing alcohol increases, the melting temperature of globular proteins decreases at constant alcohol concentrations. If the chain is branched or an additional hydroxyl substituent is present, the denaturing effect is diminished, which suggests that hydrophobic interactions between the cosolvent and protein are important for denaturation of tertiary structure 22. In fact, it is often noted that alcohols denature proteins by decreasing global hydrophobic interactions through solvation of hydrophobic amino acids and increasing local hydrogen bonding, particularly where helical tendencies exist 14, 23–25.…”

Section: Discussionmentioning

confidence: 99%

Metal‐catalyzed oxidation of human growth hormone: Modulation by solvent‐induced changes of protein conformation

Hovorka

Hong

Cleland

et al. 2001

Journal of Pharmaceutical Sciences

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“…16 The hydrophobic interactions are important stabilization factor of the collagen structure. 17 In water, pairs of nonpolar groups experience an attraction with one another by the hydrophobic interaction. 18 Since, the collagen hydrogel contain fixed proportion of water, in this system, water/hydrophilic groups/ hydrophobic chain segments maintain balance of the whole system, which made the hydrophobic chain segments stretch.…”

Section: Deswelling Behavior Of Collagen Hydrogel In Aqueous Mediamentioning

confidence: 99%

Stimuli responsive deswelling of radiation synthesized collagen hydrogel in simulated physiological environment

Zhang

Wei

et al. 2012

J Biomedical Materials Res

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Collagen hydrogels were prepared via radiation crosslinking. The simulated physiological environmental effects related to their biomedical applications on the volume phase transition of collagen hydrogel were studied, that is stimuli response to ions, temperature, and pH. The deswelling behavior of collagen hydrogel depends on the salt concentration, temperature, pH, and the hydrogel preparation procedure. Meanwhile, hydrogel structure related to the volume phase transition was investigated by FTIR, fluorescence spectrum, and HR-MAS NMR. Deswelling in salt solution caused little change on collagen conformation, and a denser network led to more significant tyrosine-derived fluorescence quenching. Hydrogen bonding between hydrated water and collagen polypeptide chain was dissociated and the activity of hydrophobic side chain increased, inducing a higher extent of contraction with the increasing of salt concentration. Moreover, salt solution treatments weakened the electrostatic interactions, side chains interactions, and hydrogen bonding of collagen hydrogel, which reduced the thermal stability of collagen hydrogel. Comparing with cell-free collagen hydrogel contraction, fibroblasts did not aggravate contraction of collagen hydrogel significantly. This study elucidated the deswelling mechanism of radiation crosslinked collagen hydrogel in simulated physiological environment and provides strategies for controlling the stimuli response of collagen hydrogel in biomedical application.

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Evidence for the existence of hydrophobic interactions as a stabilizing factor in collagen structure

Cited by 33 publications

References 15 publications

Effect of alcohols and neutral salt on the thermal stability of soluble and precipitated acid-soluble collagen

Effect of alcohols and neutral salt on the thermal stability of soluble and precipitated acid-soluble collagen

Metal‐catalyzed oxidation of human growth hormone: Modulation by solvent‐induced changes of protein conformation

Stimuli responsive deswelling of radiation synthesized collagen hydrogel in simulated physiological environment

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