What question did this study set out to answer?

To examine the conformational behavior and disruption of β-sheet aggregates in resin-bound protected peptides and determine how individual amino acid residues dictate structural stability.

March 1, 1989Bulletin of the Chemical Society of Japan

Individuality of Amino Acid Residues in Protected Peptides. Conformational and β-Sheet Structure-Disrupted Behaviors of Resin-Bound Peptides

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Authors

MNMitsuaki NaritaNihon Pharmaceutical University SIShizuko IsokawaDr Emilio B Espinosa Sr Memorial State College of Agriculture and Technology SHShinya HondaPeptidream (Japan)

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Implication

Spectroscopic study reveals amino acid composition governs beta-sheet disruption in resin-bound peptides, indicating intrinsic conformational tendencies control aggregation behavior.

Key Points

To examine the conformational behavior and disruption of β-sheet aggregates in resin-bound protected peptides and determine how individual amino acid residues dictate structural stability.
Swelled cross-linked polystyrene resin-bound peptides in dichloromethane and analyzed their secondary conformations using infrared absorption spectroscopy.
Conducted solvent titration experiments using hexafluoroisopropanol (HFIP) across pentapeptides and longer peptide chains to monitor the disruption of intermolecular hydrogen bonding.
Calculated average conformational potential parameters for α-helix (〈Pα〉), β-sheet (〈Pβ〉), and coil structure (〈Pc〉) to evaluate resistance to β-sheet disruption.
All examined resin-bound peptides readily formed aggregated β-sheet structures through intermolecular hydrogen bonding in dichloromethane.
Pentapeptide β-sheets dissociated readily with small amounts of HFIP, whereas disruption in larger peptides varied according to specific amino acid compositions.
Peptides with a coil parameter 〈Pc〉 above 0.85 or a high potential for β-sheet-to-helix transformation disrupted smoothly upon HFIP addition, whereas those lacking these potentials resisted disruption.

Cite This Study

Narita et al. (1989) studied this question.

synapsesocial.com/papers/6a982b54b66eb566e1fa9b28 https://doi.org/10.1246/bcsj.62.773

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Implication

Spectroscopic study reveals amino acid composition governs beta-sheet disruption in resin-bound peptides, indicating intrinsic conformational tendencies control aggregation behavior.

Individuality of Amino Acid Residues in Protected Peptides. Conformational and β-Sheet Structure-Disrupted Behaviors of Resin-Bound Peptides

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Implication

Key Points

Cite This Study

Individuality of Amino Acid Residues in Protected Peptides. Conformational and β-Sheet Structure-Disrupted Behaviors of Resin-Bound Peptides

Discussion

Member takes

Implication

Key Points

Cite This Study

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