Self-organization of short peptide fragments: from amyloid fibrils to nanoscale supramolecular assemblies

S Gilead, E Gazit - Supramolecular Chemistry, 2005 - Taylor & Francis
Numerous supramolecular protein assemblies had been demonstrated to have either
physiological or pathological activities. The most significant case of disease-associated self …

A near‐infrared probe for detecting and interposing amyloid beta oligomerization in early Alzheimer's disease

L Quan, I Moreno‐Gonzalez, Z Xie… - Alzheimer's & …, 2023 - Wiley Online Library
Background The misfolding and deposition of amyloid beta (Aβ) in human brain is the main
hallmark of Alzheimer's disease (AD) pathology. One of the drivers of Alzheimer´ s …

Advances in Peptide-Decorated Targeted Drug Delivery: Exploring Therapeutic Potential and Nanocarrier Strategies

HS Buddhiraju, DN Yadav, S Dey, K Eswar… - ACS Applied Bio …, 2023 - ACS Publications
Peptides are ideal biologicals for targeted drug delivery and have also been increasingly
employed as theranostic tools in treating various diseases, including cancer, with minimal or …

Short peptides as tunable, switchable, and strong gelators

R Schweitzer-Stenner, NJ Alvarez - The Journal of Physical …, 2021 - ACS Publications
This Perspective outlines our current understanding of molecular gels composed of short
and ultrashort peptides over the past 20 years. We discuss in detail the state of the art …

Bio-inspired amyloid polypeptides: From self-assembly to nanostructure design and biotechnological applications

Y Lai, F Li, Z Zou, M Saeed, Z Xu, H Yu - Applied Materials Today, 2021 - Elsevier
The aggregation of amyloid polypeptide plays a crucial role in inducing various chronic
diseases, such as neurodegenerative diseases and type II diabetes. Up to date, amyloid …

αA-Crystallin Peptide 66SDRDKFVIFLDVKHF80 Accumulating in Aging Lens Impairs the Function of α-Crystallin and Induces Lens Protein Aggregation

P Santhoshkumar, M Raju, KK Sharma - PloS one, 2011 - journals.plos.org
Background The eye lens is composed of fiber cells that are filled with α-, β-and γ-crystallins.
The primary function of crystallins is to maintain the clarity of the lens through ordered …

The self-assembling zwitterionic form of L-phenylalanine at neutral pH

E Mossou, SCM Teixeira, EP Mitchell… - … Section C: Structural …, 2014 - journals.iucr.org
The title zwitterion (2S)-2-azaniumyl-1-hydroxy-3-phenylpropan-1-olate, C9H11NO2, also
known as l-phenylalanine, was characterized using synchrotron X-rays. It crystallized in the …

Pristine and hydroxylated fullerenes prevent the aggregation of human islet amyloid polypeptide and display different inhibitory mechanisms

C Bai, Z Lao, Y Chen, Y Tang, G Wei - Frontiers in Chemistry, 2020 - frontiersin.org
Protein aggregation, involving the formation of dimers, oligomers, and fibrils, is associated
with many human diseases. Type 2 diabetes is one of the common amyloidosis and linked …

Molecular dynamics simulations on the oligomer-formation process of the GNNQQNY peptide from yeast prion protein Sup35

Z Zhang, H Chen, H Bai, L Lai - Biophysical journal, 2007 - cell.com
Oligomeric intermediates are possible cytotoxic species in diseases associated with amyloid
deposits. Understanding the early steps of fibril formation at atomic details may provide …

Amino acid metaclusters: implications of growth trends on peptide self-assembly and structure

TD Do, NEC De Almeida, NE LaPointe… - Analytical …, 2016 - ACS Publications
Ion-mobility mass spectrometry is utilized to examine the metacluster formation of serine,
asparagine, isoleucine, and tryptophan. These amino acids are representative of different …