Polymers of tripeptides as collagen models

Engel, Jürgen; Kurtz, Joseph; Katchalski, Ephraim; Berger, Arieh

doi:10.1016/s0022-2836(66)80106-7

Cited by 146 publications

(54 citation statements)

References 33 publications

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“…Limited proteolytic digestion with papain and pepsin has also been used to solubilize type II collagen from bovine articular cartilage and from normal chick sternal cartilage (Strawich and . Type III collagen can be extracted from skin and blood vessel walls by limited digestion with pepsin Epstein, 1974;.…”

Section: Extraction From Tissuesmentioning

confidence: 99%

The Chemistry and Biology of Collagen

Börnstein¹,

Traub²

1979

The Proteins

183

119

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Section: Extraction From Tissuesmentioning

confidence: 99%

The Chemistry and Biology of Collagen

Börnstein¹,

Traub²

1979

The Proteins

183

119

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“…These latter workers employed solid phase synthesis with t-amyloxycarbonyl-ProPro-Gly-as the basic addition unit. The reported physical properties of their (Pro-Pro-Gly), polymer^^-^ differed substantially from those polymers of comparable molecular weight of Engel et al 3 The polymers of Sakakibara et a1. 4 were less water soluble and exhibited much sharper melting profiles with significantly greater total change in optical rotation.…”

Section: Introductionmentioning

confidence: 77%

The association reaction of collagen model polypeptides (Pro‐Pro‐Gly)_n

Shaw

Schurr

1975

Biopolymers

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SynopsisThe characterization of recently synthesized (Pro-Pro-Gly),, n = 7 , s is described, along with melting profile studies of its association equilibrium, and thermal quenching studies of the kinetics of its association reaction. The order of the kinetic reaction is about 3, implying that three peptide chains are involved in the activated state of the rate-limiting step. The reaction rate was found to exhibit a negative temperature coefficient. With the (Pro-Pro-Gly)7 peptide, the concentration dependence of the (Pro-Pro-Gly), association equilibrium was observed for the first time.Detailed thermodynamic analysis for these n = 7, 8 data, together with literature data for n = 10, 15,20 were carried out for both the simple "all-or-none" binding model and for a series of complex equilibrium models. For the latter, all of the (Pro-Pro-Gly), data (in 10% acetic acid) are fit best with a maximally cooperative near-neighbor model with a standard enthalpy change AH = -650 cal/mole of residues, and a standard entropy change A S = -14.63 -.10/n cal/deg-mole of residues, wherein the -10 eu represents an end-effect contribution to the binding free energy.With regard to optical rotatory properties and thermodynamic parameters, the data for the new n = 7, 8 peptides match rather well with the literature data for the n = 10, 15, and 20 peptides.The enthalpic stabilization per residue of the triple-helical form of (Pro-Pro-Gly), was nearly an order of magnitude smaller than the enthalpic stabilization per additional proline obtained from diwct calorimetric measurements on native collagens of different (and much lower) proline contents by Privalov and Tiktopulo. [Biopolyrners (1970) 9, 127-139.1 Possible explanations for this phenomenon are discussed.

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“…I n fact, ORD spectra of poly(Pro-Pro-Gly) and CD spectra of poly (Pro-Ala-Gly) were similar to those of ~ollagen.~~S However, because of the heterogeneity of the peptides, the direct measurement of molecular weights to determine the number of polypeptide chains making up the ordered structure in the solution led to somewhat confusing results. 6 On the other hand, a solution of poly(A1a-Pro-Gly), which did not form a triple-helical structure in the solid state, showed no change of optical rotation on ~a r m i n g .~ This suggests that the peptide remains disordered in the temperature range studied.…”

mentioning

confidence: 94%

Conformational change of the triple‐helical structure. II. Conformation of (Pro‐Pro‐Gly)_n and (Pro‐Pro‐Gly)_n(Ala‐Pro‐Gly)_m(Pro‐Pro‐Gly)_n in an aqueous solution

Sutoh¹,

Noda²

1974

Biopolymers

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Measurements of the molecular weight of (Pro‐Pro‐Gly)n and (Pro‐Pro‐Gly)n(Ala‐Pro‐Gly)m(Pro‐Pro‐Gly)n, which were synthesized by the solid‐phase method, revealed that they formed a trimer in an aqueous solution, and dissociated into single‐stranded chains on warming. Accompanying the transition, a large decrease of optical rotation was observed, like the collagen–gelatin transition. The shape of the trimeric molecule was rodlike, and the dimensions were 12 Å in diameter and 2.8 Å per residue in length, regardless of the length of Ala‐Pro‐Gly sequences in a peptide chain. The data indicate that both Pro‐Pro‐Gly sequences and Ala‐Pro‐Gly sequences from the triple‐helical structure similar to that of collagen in aqueous solution. All optical rotational dispersion (ORD) curves of solutions of the peptides were represented by a single‐term Drude equation, and the Drude constant λc was 200 nm for all peptides regardless of the length of Ala‐Pro‐Gly sequences. The resemblance between the helical structure formed by Pro‐Pro‐Gly sequences and that by Ala‐Pro‐Gly sequences was also suggested by the formation of the hybrid triple helix from two kinds of peptide chains with different lengths of Ala‐Pro‐Gly sequences.

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Polymers of tripeptides as collagen models

Cited by 146 publications

References 33 publications

The Chemistry and Biology of Collagen

The Chemistry and Biology of Collagen

The association reaction of collagen model polypeptides (Pro‐Pro‐Gly)_n

Conformational change of the triple‐helical structure. II. Conformation of (Pro‐Pro‐Gly)_n and (Pro‐Pro‐Gly)_n(Ala‐Pro‐Gly)_m(Pro‐Pro‐Gly)_n in an aqueous solution

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Polymers of tripeptides as collagen models

Cited by 146 publications

References 33 publications

The Chemistry and Biology of Collagen

The Chemistry and Biology of Collagen

The association reaction of collagen model polypeptides (Pro‐Pro‐Gly)n

Conformational change of the triple‐helical structure. II. Conformation of (Pro‐Pro‐Gly)n and (Pro‐Pro‐Gly)n(Ala‐Pro‐Gly)m(Pro‐Pro‐Gly)n in an aqueous solution

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The association reaction of collagen model polypeptides (Pro‐Pro‐Gly)_n

Conformational change of the triple‐helical structure. II. Conformation of (Pro‐Pro‐Gly)_n and (Pro‐Pro‐Gly)_n(Ala‐Pro‐Gly)_m(Pro‐Pro‐Gly)_n in an aqueous solution