Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Growth, Polymorphism, and Spatially Controlled Surface Immobilization of Biotinylated Variants of IAPP21-27 Fibrils.

Biomacromolecules - 10 Feb 2020

John Torsten, Bandak Juhaina, Sarveson Nilushiya, Hackl Claudia, Risselada Herre Jelger, Prager Andrea, Elsner Christian, Abel Bernd

Abstract excerpt

The islet amyloid polypeptide (IAPP) is a regulatory peptide that can aggregate into fibrillar structures associated with type 2 diabetes. In this study, the IAPP21-27 segment was modified with a biotin linker at the N-terminus (Btn-GNNFGAIL) to immobilize peptide fibrils on streptavidin-coated surfaces. Key residues for fibril formation of the N-terminal biotinylated IAPP21-27 segment were identified by using an...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Biotinylation
Share to Genetic Variation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Islet Amyloid Polypeptide

Share to Peptide Fragments

Share to Polymorphism, Genetic

Share to Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Share to Surface Properties

Source

Identifiers

PMID: 31887030
DOI: 10.1021/acs.biomac.9b01466

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Growth, Polymorphism, and Spatially Controlled Surface Immobilization of Biotinylated Variants of IAPP21-27 Fibrils.PMID 31887030Read ↗

Tracking the amyloidogenic core of IAPP amyloid fibrils: Insights from micro-Raman spectroscopy.Semantic proximity Read ↗

Peptide sequence and amyloid formation; molecular simulations and experimental study of a human islet amyloid polypeptide fragment and its analogs.Semantic proximity Read ↗

Distal amyloid β-protein fragments template amyloid assembly.Semantic proximity Read ↗

Design of amyloidogenic peptide trapsSemantic proximity Read ↗

Controlling self-assembly of engineered peptides on graphite by rational mutation.Semantic proximity Read ↗

Heterogeneous triangular structures of human islet amyloid polypeptide (amylin) with internal hydrophobic cavity and external wrapping morphology reveal the polymorphic nature of amyloid fibrils.Semantic proximity Read ↗

A Protocol for the Design of Protein and Peptide Nanostructure Self-Assemblies Exploiting Synthetic Amino Acids.Semantic proximity Read ↗

Beta structure motifs of islet amyloid polypeptides identified through surface-mediated assemblies.Semantic proximity Read ↗

Massively parallel quantification of mutational impact on IAPP amyloid formation.Semantic proximity Read ↗

Peptides that form β-sheets on hydrophobic surfaces accelerate surface-induced insulin amyloidal aggregation.Semantic proximity Read ↗

Massively parallel quantification of mutational impact on IAPP amyloid formationSemantic proximity Read ↗

Amyloid fibril structure of islet amyloid polypeptide by cryo-electron microscopy reveals similarities with amyloid betaSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.