Structure and dynamics of interfacial peptides and proteins from vibrational sum-frequency generation spectroscopy

S Hosseinpour, SJ Roeters, M Bonn, W Peukert… - Chemical …, 2020 - ACS Publications
Proteins at interfaces play important roles in cell biology, immunology, bioengineering, and
biomimetic material design. Many biological processes are based on interfacial protein …

Elevated concentrations cause upright alpha-synuclein conformation at lipid interfaces

SJ Roeters, K Strunge, KB Pedersen… - Nature …, 2023 - nature.com
The amyloid aggregation of α-synuclein (α S), related to Parkinson's disease, can be
catalyzed by lipid membranes. Despite the importance of lipid surfaces, the 3D-structure and …

Developments and ongoing challenges for analysis of surface-bound proteins

T Weidner, DG Castner - Annual Review of Analytical Chemistry, 2021 - annualreviews.org
Proteins at surfaces and interfaces play important roles in the function and performance of
materials in applications ranging from diagnostic assays to biomedical devices. To improve …

Orientation and conformation of proteins at the air–water interface determined from integrative molecular dynamics simulations and sum frequency generation …

S Alamdari, SJ Roeters, TW Golbek, L Schmüser… - Langmuir, 2020 - ACS Publications
Understanding the assembly of proteins at the air-water interface (AWI) informs the formation
of protein films, emulsion properties, and protein aggregation. Determination of protein …

Acidic PH Promotes Refolding and Macroscopic Assembly of Amyloid β (16–22) Peptides at the Air–Water Interface

H Lu, L Bellucci, S Sun, D Qi, M Rosa… - The Journal of …, 2022 - ACS Publications
Assembly by amyloid-beta (Aβ) peptides is vital for various neurodegenerative diseases.
The process can be accelerated by hydrophobic interfaces such as the cell membrane …

Acidic environment significantly alters aggregation pathway of human islet amyloid polypeptide at negative lipid membrane

J Zhang, J Tan, R Pei, S Ye - Langmuir, 2020 - ACS Publications
The misfolding and aggregation of human islet amyloid polypeptide (hIAPP) at cell
membrane has a close relationship with the development of type 2 diabetes (T2DM). This …

Umbrella-like helical structure of α-synuclein at the air–water interface observed with experimental and theoretical sum frequency generation spectroscopy

K Strunge, T Burgin, TW Golbek… - The Journal of …, 2023 - ACS Publications
The misfolding of α-synuclein (αS) into amyloid aggregates is catalyzed by hydrophobic
surfaces and associated with severe brain disorders, such as Parkinson's disease. Despite …

Biomineralization at fluid interfaces

M Cano, JJ Giner-Casares - Advances in Colloid and Interface Science, 2020 - Elsevier
Biomineralization is of paramount importance for life on Earth. The delicate balance of
physicochemical interactions at the interface between organic and inorganic matter during …

Backbone structure of diatom silaffin peptide R5 in biosilica determined by combining solid-state nmr with theoretical sum-frequency generation spectra

SJ Roeters, R Mertig, H Lutz, A Roehrich… - The journal of …, 2021 - ACS Publications
Silaffin peptide R5 is key for the biogenesis of silica cell walls of diatoms. Biosilification by
the R5 peptide has potential in biotechnology, drug development, and materials science due …

Hydroxyapatite formation on self-assembling peptides with differing secondary structures and their selective adsorption for proteins

S Kojima, H Nakamura, S Lee, F Nagata… - International Journal of …, 2019 - mdpi.com
Self-assembling peptides have been employed as biotemplates for biomineralization, as the
morphologies and sizes of the inorganic materials can be easily controlled. We synthesized …