New Insights from Sum Frequency Generation Vibrational Spectroscopy into the Interactions of Islet Amyloid Polypeptides with Lipid Membranes

Fu, Li; Wang, Zhuguang; Batista, Victor S.; Yan, Elsa C.  Y.

doi:10.1155/2016/7293063

Title: New Insights from Sum Frequency Generation Vibrational Spectroscopy into the Interactions of Islet Amyloid Polypeptides with Lipid Membranes

Journal Article · Fri Jan 01 00:00:00 EST 2016 · Journal of Diabetes Research

DOI:https://doi.org/10.1155/2016/7293063· OSTI ID:1626231

^[1]; Wang, Zhuguang ^[2]; Batista, Victor S. ^[2]; Yan, Elsa C. Y. ^[2]

Pacific Northwest National Laboratory (PNNL), Richland, WA (United States). William R. Wiley Environmental Molecular Sciences Laboratory
Yale Univ., New Haven, CT (United States). Dept. of Chemistry

Studies of amyloid polypeptides on membrane surfaces have gained increasing attention in recent years. Several studies have revealed that membranes can catalyze protein aggregation and that the early products of amyloid aggregation can disrupt membrane integrity, increasing water permeability and inducing ion cytotoxicity. Nonetheless, probing aggregation of amyloid proteins on membrane surfaces is challenging. Surface-specific methods are required to discriminate contributions of aggregates at the membrane interface from those in the bulk phase and to characterize protein secondary structuresin situand in real time without the use of perturbing spectroscopic labels. Here, we review the most recent applications of sum frequency generation (SFG) vibrational spectroscopy applied in conjunction with computational modeling techniques, a joint experimental and computational methodology that has provided valuable insights into the aggregation of islet amyloid polypeptide (IAPP) on membrane surfaces. These applications show that SFG can provide detailed information about structures, kinetics, and orientation of IAPP during interfacial aggregation, relevant to the molecular mechanisms of type II diabetes. These recent advances demonstrate the promise of SFG as a new approach for studying amyloid diseases at the molecular level and for the rational drug design targeting early aggregation products on membrane surfaces.

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Research Organization:: Pacific Northwest National Lab (PNNL), Richland, WA (United States)

Sponsoring Organization:: USDOE Office of Science (SC); Spectroscopy Society of Pittsburgh; National Science Foundation (NSF); National Institutes of Health (NIH)

Grant/Contract Number:: AC05-76RL01830; CHE-1213362; 1R56DK105381-01; CHE-1213742

OSTI ID:: 1626231

Journal Information:: Journal of Diabetes Research, Vol. 2016; ISSN 2314-6745

Country of Publication:: United States

Language:: English

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Revealing a Dual Role of Ganglioside Lipids in the Aggregation of Membrane-Associated Islet Amyloid Polypeptide Christensen, Mikkel; Schiøtt, Birgit The Journal of Membrane Biology, Vol. 252, Issue 4-5 https://doi.org/10.1007/s00232-019-00074-5	journal	June 2019
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High speed atomic force microscopy to investigate the interactions between toxic Aβ _1-42 peptides and model membranes in real time: impact of the membrane composition Ewald, M.; Henry, S.; Lambert, E. Nanoscale, Vol. 11, Issue 15 https://doi.org/10.1039/c8nr08714h	journal	January 2019

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