scholarly journals Fibrillar dimer formation of islet amyloid polypeptides

AIP Advances ◽  
2015 ◽  
Vol 5 (9) ◽  
pp. 092501 ◽  
Author(s):  
Chi-cheng Chiu ◽  
Juan J. de Pablo
Keyword(s):  
Islet Amyloid ◽  
Dimer Formation ◽  
Amyloid Polypeptides

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

2016 ◽  
Vol 2016 ◽  
pp. 1-17 ◽  
Author(s):  
Li Fu ◽  
Zhuguang Wang ◽  
Victor S. Batista ◽  
Elsa C. Y. Yan
Keyword(s):  
Vibrational Spectroscopy ◽  
Molecular Mechanisms ◽  
Membrane Integrity ◽  
Sum Frequency Generation ◽  
Islet Amyloid ◽  
Sum Frequency ◽  
Protein Secondary Structures ◽  
Membrane Surfaces ◽  
Frequency Generation ◽  
Amyloid Polypeptides

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.

Antimicrobial activity of human islet amyloid polypeptides: an insight into amyloid peptides’ connection with antimicrobial peptides

2012 ◽  
Vol 393 (7) ◽  
pp. 641-646 ◽  
Author(s):  
Lan Wang ◽  
Qian Liu ◽  
Jin-Chun Chen ◽  
Yi-Xian Cui ◽  
Bing Zhou ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Antimicrobial Peptides ◽  
Lipid Membrane ◽  
Human Islet ◽  
Amyloid Peptide ◽  
Islet Amyloid ◽  
Amyloid Peptides ◽  
Amyloid Polypeptides ◽  
New Evidence ◽  
Insight Into

Abstract Human islet amyloid polypeptide (hIAPP) shows an antimicrobial activity towards two types of clinically relevant bacteria. The potency of hIAPP varies with its aggregation states. Circular dichroism was employed to determine the interaction between hIAPP and bacteria lipid membrane mimic. The antimicrobial activity of each aggregate species is associated with their ability to induce membrane disruption. Our findings provide new evidence revealing the antimicrobial activity of amyloid peptide, which suggest a possible connection between amyloid peptides and antimicrobial peptides.

scholarly journals Membrane Permeation Induced by Aggregates of Human Islet Amyloid Polypeptides

2013 ◽  
Vol 105 (10) ◽  
pp. 2323-2332 ◽  
Author(s):  
Chetan Poojari ◽  
Dequan Xiao ◽  
Victor S. Batista ◽  
Birgit Strodel
Keyword(s):  
Human Islet ◽  
Membrane Permeation ◽  
Islet Amyloid ◽  
Amyloid Polypeptides

Enhanced optical asymmetry in supramolecular chiroplasmonic assemblies with long-range order

Science ◽  
2021 ◽  
Vol 371 (6536) ◽  
pp. 1368-1374 ◽  
Author(s):  
Jun Lu ◽  
Yao Xue ◽  
Kalil Bernardino ◽  
Ning-Ning Zhang ◽  
Weverson R. Gomes ◽  
...  
Keyword(s):  
Long Range ◽  
Gold Nanorods ◽  
Spectral Shift ◽  
Human Islet ◽  
Range Order ◽  
Long Range Order ◽  
Islet Amyloid ◽  
Strong Polarization ◽  
Amyloid Polypeptides ◽  
Strong Scattering

Chiral assemblies of plasmonic nanoparticles are known for strong circular dichroism but not for high optical asymmetry, which is limited by the unfavorable combination of electrical and magnetic field components compounded by strong scattering. Here, we show that these limitations can be overcome by the long-range organization of nanoparticles in a manner similar to the liquid crystals and found in helical assemblies of gold nanorods with human islet amyloid polypeptides. A strong, polarization-dependent spectral shift and the reduced scattering of energy states with antiparallel orientation of dipoles activated in assembled helices increased optical asymmetry g-factors by a factor of more than 4600. The liquid crystal–like color variations and the nanorod-accelerated fibrillation enable drug screening in complex biological media. Improvement of long-range order can also provide structural guidance for the design of materials with high optical asymmetry.

Glycated Insulin Exacerbates the Cytotoxicity of Human Islet Amyloid Polypeptides: a Vicious Cycle in Type 2 Diabetes

2019 ◽  
Vol 14 (3) ◽  
pp. 486-496 ◽  
Author(s):  
Liang Ma ◽  
Chen Yang ◽  
Lianqi Huang ◽  
Yuchen Chen ◽  
Yang Li ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Human Islet ◽  
Vicious Cycle ◽  
Islet Amyloid ◽  
Amyloid Polypeptides

Cross-Sequence Interactions between Human and Rat Islet Amyloid Polypeptides

Langmuir ◽  
2014 ◽  
Vol 30 (18) ◽  
pp. 5193-5201 ◽  
Author(s):  
Rundong Hu ◽  
Mingzhen Zhang ◽  
Kunal Patel ◽  
Qiuming Wang ◽  
Yung Chang ◽  
...  
Keyword(s):  
Islet Amyloid ◽  
Amyloid Polypeptides
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