What question did this study set out to answer?

Evaluate the conformational structures and β-sheet aggregation tendencies of human proinsulin C-peptide fragments anchored to polystyrene resins during solid-phase synthesis.

April 1, 1988Bulletin of the Chemical Society of JapanOpen Access

Infrared Spectroscopic Conformational Analysis of Polystyrene Resin-Bound Human Proinsulin C-Peptide Fragments. β-Sheet Aggregation of Peptide Chains during Solid-Phase Peptide Synthesis

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Authors

MNMitsuaki NaritaNihon Pharmaceutical University SHShinya HondaPeptidream (Japan)HUHiroshi UmeyamaToppan (Japan)

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Implication

Spectroscopic analysis demonstrates beta-sheet aggregation in resin-bound proinsulin C-peptide fragments, indicating intermolecular hydrogen bonding challenges during solid-phase peptide synthesis.

Key Points

Evaluate the conformational structures and β-sheet aggregation tendencies of human proinsulin C-peptide fragments anchored to polystyrene resins during solid-phase synthesis.
Analyzed octa- and tridecapeptide fragments bound to soluble and cross-linked polystyrene matrices in swollen and solid states using infrared absorption spectroscopy.
Predicted β-sheet aggregation potential using average coil conformational values (〈Pc〉) and evaluated the structural effects of mechanical shear stress in the solid state.
Both octa- and tridecapeptides readily engaged in intermolecular hydrogen bonding to form β-sheet aggregates, even at low peptide loading densities on the resin.
Resin-bound peptides exhibited a high propensity for β-sheet formation comparable to free peptides lacking macromolecular protecting groups, in agreement with calculated 〈Pc〉 values.

Cite This Study

Narita et al. (1988) studied this question.

synapsesocial.com/papers/6a982b54b66eb566e1fa9b2a https://doi.org/10.1246/bcsj.61.1201

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Implication

Spectroscopic analysis demonstrates beta-sheet aggregation in resin-bound proinsulin C-peptide fragments, indicating intermolecular hydrogen bonding challenges during solid-phase peptide synthesis.

Infrared Spectroscopic Conformational Analysis of Polystyrene Resin-Bound Human Proinsulin C-Peptide Fragments. β-Sheet Aggregation of Peptide Chains during Solid-Phase Peptide Synthesis

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Cite This Study

Infrared Spectroscopic Conformational Analysis of Polystyrene Resin-Bound Human Proinsulin C-Peptide Fragments. β-Sheet Aggregation of Peptide Chains during Solid-Phase Peptide Synthesis

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