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Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

Published on: March 24, 2017

Targeting S100B with Peptides Encoding Intrinsic Aggregation-Prone Sequence Segments.

Joana S Cristóvão^1,2, Mariana A Romão^1,2, Rodrigo Gallardo^3,4

¹Biosystems and Integrative Sciences Institute, Faculdade de Ciências, Universidade Lisboa, 1749-016 Lisbon, Portugal.

Molecules (Basel, Switzerland)

|January 20, 2021

Summary

This summary is machine-generated.

Researchers designed S100B-derived peptides targeting aggregation-prone regions (APRs). These peptides show strong aggregation, interact with S100B, and may inhibit its function through co-aggregation, offering pharmacological potential.

Keywords:

S100 proteins amyloid protein aggregation protein biophysics structural biology

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Area of Science:

Biochemistry
Molecular Biology
Pharmacology

Background:

S100 proteins, including S100B, can form large ordered self-assemblies affecting their structure and function.
S100B is prone to β-aggregation under destabilizing conditions, with aggregation-prone regions (APRs) typically shielded at the homodimer interface.

Purpose of the Study:

To design and synthesize S100B-derived peptides targeting its APRs for potential pharmacological applications.
To investigate the aggregation propensity and S100B interaction of these synthetic peptides.

Main Methods:

Computational identification of APRs in S100B using the TANGO algorithm.
Design and synthesis of S100B-derived APR peptides.
Characterization using fluorescence spectroscopy, transmission electron microscopy, biolayer interferometry, and aggregation kinetics.

Main Results:

Synthetic peptides exhibited significant aggregation propensity.
Peptides were shown to interact with S100B.
Co-aggregation reactions between peptides and S100B were observed, suggesting potential functional inhibition.

Conclusions:

S100B-derived APR peptides demonstrate potential for pharmacological intervention.
These peptides may act by modifying the S100B interactome or promoting inactivation through selective aggregation.
Further research could explore their therapeutic applications in various physiological and pathological conditions involving S100B.