Folded β‐turns and collagenlike conformations of ‐Gly‐Pro‐ and ‐Pro‐Gly‐sequences in synthetic polytripeptides

Tamburro, Antonio Mario; Guantieri, Valeria

doi:10.1002/bip.360230403

Cited by 9 publications

(6 citation statements)

References 20 publications

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“…We also noted that addition of either ethylene glycol or HFIP/water mixtures to solution of the polypeptide did not induce a 31-helix structure typical for polyproline (Ref. 14,15). We propose that a 165 helix with 113' rotation per residue may be a better model than a 31 helix.…”

Section: Top: Differential Scanning Calorimetric Trace Bottom: Tmentioning

confidence: 70%

Design and synthesis of polytripeptide (leuglnpro)n based upon the matrix protein amelogenin

Sogah¹,

Perle-Treves²,

Voyer³

et al. 1994

Macromolecular Symposia

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A linear neutral repetitive peptide, (Leu‐Gln‐Pro)n (n = 1‐100), an analog of the Ca2+ ion‐binding domain of the matrix protein, amelogenin, has been synthesized. The polypeptide is mostly unordered in trifluoroethanol (TFE) at 25°C and its circular dichroism (CD) spectrum resembles that of the protein itself. In TFE the CD spectrum of (Leu‐Gln‐Pro)n reveals that the polypeptide interacts strongly with divalent cations Mg2+, Ca2+, Sr2+, and Ba2+ accompanied by conformational rearrangement from a random to a more‐ordered one. In the presence of Li+, Na+ and K+ ions no such conformational change has been observed. The CD curves of the complexes suggest the presence of type I β‐turns and reinforce the hypothesis that the region Gln112‐Leu138 in amelogenin is the Ca2+‐binding domain. In the solid state, powder X‐ray diffraction suggests that the polymeric (LQP)n may exist as isolated “rigid rods”.

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Section: Top: Differential Scanning Calorimetric Trace Bottom: Tmentioning

confidence: 70%

Design and synthesis of polytripeptide (leuglnpro)n based upon the matrix protein amelogenin

Sogah¹,

Perle-Treves²,

Voyer³

et al. 1994

Macromolecular Symposia

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“…For PGV in VPGVG, valine is likely to form more PPII than leucine or alanine in the same structural position, which tend to favor β-turns. 39,40 CD spectra from previous studies with SynB1-ELP show a negative peak at 195 nm, a positive peak at 210 nm, and a second negative peak at 225 nm. This combination has been shown to occur in VPGVG polypeptides with extended chain and type II-β-turns when assigning them to a class B β-turn spectra.…”

Section: Discussionmentioning

confidence: 83%

FT-IR Spectroscopic Analysis of the Secondary Structures Present during the Desiccation Induced Aggregation of Elastin-Like Polypeptide on Silica

et al. 2020

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Previously, we found that elastin-like polypeptide (ELP), when dried above the lower critical solution temperature on top of a hydrophilic fused silica disk, exhibited a dynamic coalescence behavior. The ELP initially wet the silica, but over the next 12 h, dewett the surface and formed aggregates of precise sizes and shapes. Using Fourier-transform infrared (FT-IR) spectroscopy, the present study explores the role of secondary structures present in ELP during this progressive desiccation and their effect on aggregate size. The amide I peak (1600–1700 cm–1) in the ELP’s FT-IR spectrum was deconvoluted using the second derivative method into eight subpeaks (1616, 1624, 1635, 1647, 1657, 1666, 1680, 1695 cm–1). These peaks were identified to represent extended strands, β-turns, 3(10)-helix, polyproline I, and polyproline II using previous studies on ELP and molecules similar in peptide composition. Positive correlations were established between the various subpeaks, water content, and aggregate size to understand the contributions of the secondary structures in particle formation. The positive correlations suggest that type II β-turns, independent of the water content, contributed to the growth of the aggregates at earlier time points (1–3.5 h). At later time points (6–12 h), the aggregate growth was attributed to the formation of 3(10)-helices that relied on a decrease in water content. Understanding these relationships gives greater control in creating precisely sized aggregates and surface coatings with varying roughness.

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“…Although the findings of Tamburro and Guantieri [43] that chain reversals may result in such a graphic shape we assume that the formation of ig-sheets, characterized by similar CD-spectra [44,45], cannot be excluded. This result is supported by the correlation of the complex formation and the appearance of/~-structures as the result of a thermal denaturation found for albumin [46].…”

Section: Cd-spectra Of Gelatin-surfactant Solutionsmentioning

confidence: 74%

The modification of the triple helical structure of gelatin in aqueous solution I. The influence of anionic surfactants, pH-value, and temperature

Wüstneck¹,

Wetzel

Buder

et al. 1988

Colloid & Polymer Sci

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The modification of the triple helical structure in aqueous gelatin solutions by changing pH and adding alkyl sulphates at 298 K and after rechilling the solution to 283 K was investigated by CD-measurement. At 298 K the triple helical content at the IEP of the gelatin has its maximum value. It is only weakly affected by adding sodium dodecyl sulphate (SDDS) at concentrations < 10 -4 M/dm 3. The unfolding of the triple helix affected by pH and SDDS is reversible by rechilling the solution. The triple helical content of gelatin solutions decreases at SDDS concentrations higher than 10 -4 M/dm 3. In all cases the decrease of the amount of triple helical structure is connected with an increase of the cis-configuration in single chains and leads to chain reversals. At sufficiently high SDDS concentrations 3-sheets are formed. These changes are thermally irreversible. Sodium decyl sulphate (SDS) has a more minor influence than SDDS except in the range of the c.m.c, of SDS. At sufficiently high SDS concentrations, 3-turns appear.

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Folded β‐turns and collagenlike conformations of ‐Gly‐Pro‐ and ‐Pro‐Gly‐sequences in synthetic polytripeptides

Cited by 9 publications

References 20 publications

Design and synthesis of polytripeptide (leuglnpro)n based upon the matrix protein amelogenin

Design and synthesis of polytripeptide (leuglnpro)n based upon the matrix protein amelogenin

FT-IR Spectroscopic Analysis of the Secondary Structures Present during the Desiccation Induced Aggregation of Elastin-Like Polypeptide on Silica

The modification of the triple helical structure of gelatin in aqueous solution I. The influence of anionic surfactants, pH-value, and temperature

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