Probing Solid-Binding Peptide Self-Assembly Kinetics Using a Frequency Response Cooperativity Model DOI Creative Commons
Taylor Bader, Kyle Boone,

Chris Johnson

et al.

Biomimetics, Journal Year: 2025, Volume and Issue: 10(2), P. 107 - 107

Published: Feb. 12, 2025

Biomolecular adsorption has great significance in medical, environmental, and technological processes. Understanding equilibrium binding kinetics is essential for advanced process implementation. This requires identifying intrinsic determinants that predict optimal properties at bio-hybrid interfaces. Solid-binding peptides (SBPs) have targetable involving peptide-peptide peptide-solid interactions, which result high-affinity material-selective binding. Atomic force microscopy investigations confirmed this complex interplay of multi-step peptide assemblies a cooperative modus. Yet, most studies report SBPs using non-cooperative or single-step models. Using kinetic models predicting self-assembly behavior creates an oversimplified view adsorption, restricting implementing beyond their current use. To address these limitations provide insight into surface-level events during self-assembly, novel method, the Frequency Response Cooperativity model, was developed. model iteratively fits data through spectral analysis several time-dependent parameters. The applied to widely used gold-binding obtained quartz crystal microbalance with dissipation, verified assembly. Peak deconvolution plots revealed distinct differences size distribution rates present across concentrations. approach provides new fundamental insights intricate dynamics biomolecules on surfaces.

Language: Английский

Prebiotic Peptides: Molecular Hubs in the Origin of Life DOI
Moran Frenkel‐Pinter, Mousumi Samanta, Gonen Ashkenasy

et al.

Chemical Reviews, Journal Year: 2020, Volume and Issue: 120(11), P. 4707 - 4765

Published: Feb. 26, 2020

The fundamental roles that peptides and proteins play in today's biology makes it almost indisputable were key players the origin of life. Insofar as is appropriate to extrapolate back from extant prebiotic world, one must acknowledge critical importance interconnected molecular networks, likely with components, would have played life's origin. In this review, we summarize chemical processes involving could contributed early evolution, an emphasis on interactions between other classes organic molecules. We first mechanisms by which amino acids similar building blocks been produced elaborated into proto-peptides. Next, non-covalent well nucleic acids, lipids, carbohydrates, metal ions, aromatic molecules are discussed relation possible such evolution structure function. Finally, describe research structural alternatives covalent adducts acids/peptides propose ample future breakthroughs origin-of-life chemistry will stem investigations systems synergistic different emerge.

Language: Английский

Citations

273
The Unfolded Protein Response: Detecting and Responding to Fluctuations in the Protein-Folding Capacity of the Endoplasmic Reticulum DOI Open Access
G Elif Karagöz, Diego Acosta‐Alvear, Peter Walter

et al.

Cold Spring Harbor Perspectives in Biology, Journal Year: 2019, Volume and Issue: 11(9), P. a033886 - a033886

Published: Jan. 22, 2019

Most of the secreted and plasma membrane proteins are synthesized on membrane-bound ribosomes endoplasmic reticulum (ER). They require engagement ER-resident chaperones foldases that assist in their folding maturation. Since protein homeostasis ER is crucial for cellular function, protein-folding status organelle's lumen continually surveyed by a network signaling pathways, collectively called unfolded response (UPR). Protein-folding imbalances, or "ER stress," detected highly conserved sensors adjust ER's capacity according to physiological needs cell. We review recent developments field have provided new insights into stress-sensing mechanisms used UPR which they integrate various inputs organelle accommodate fluctuations demands.

Language: Английский

Citations

266
Production and processing of antioxidant bioactive peptides: A driving force for the functional food market DOI Creative Commons
Solomon Abebaw Tadesse,

Shimelis Admassu Emire

Heliyon, Journal Year: 2020, Volume and Issue: 6(8), P. e04765 - e04765

Published: Aug. 1, 2020

Recently, the demand for functional foods in global market has increased rapidly due to increasing occurrences of non-communicable diseases and technological advancement. Antioxidant peptides have been suggested as ingredients used produce health-promoting foods. These are encrypted from various food derived protein sources by chemical enzymatic hydrolysis, microbial fermentation. However, industrial-scale production antioxidant is hampered different problems such high cost, low yield bioactivity. Accordingly, novel processing technologies, pressure, microwave pulsed electric field, recently emerged overcome associated with conventional hydrolysis methods. This particular review, therefore, discussed current technologies peptides. The review also further perspectives that should be addressed future.

Language: Английский

Citations

188
Structure and Aggregation Mechanisms in Amyloids DOI Creative Commons
Zaida L. Almeida, Rui M. M. Brito

Molecules, Journal Year: 2020, Volume and Issue: 25(5), P. 1195 - 1195

Published: March 6, 2020

The aggregation of a polypeptide chain into amyloid fibrils and their accumulation deposition insoluble plaques intracellular inclusions is the hallmark several misfolding diseases known as amyloidoses. Alzheimer's, Parkinson's Huntington's are some approximately 50 described to date. identification characterization molecular species critical for formation disease development have been focus intense scrutiny. Methods such X-ray electron diffraction, solid-state nuclear magnetic resonance spectroscopy (ssNMR) cryo-electron microscopy (cryo-EM) extensively used they contributed shed new light onto structure amyloid, revealing multiplicity polymorphic structures that generally fit cross-β motif. rational therapeutic approaches against these debilitating increasingly frequent requires thorough understanding mechanisms underlying cascade. Here, we review current knowledge on fibril proteins peptides from kinetic thermodynamic point view, involved in amyloidogenic process, origin cytotoxicity.

Language: Английский

Citations

174
A guide to studying protein aggregation DOI Open Access
Joëlle A.J. Housmans, Guiqin Wu, Joost Schymkowitz

et al.

FEBS Journal, Journal Year: 2021, Volume and Issue: 290(3), P. 554 - 583

Published: Dec. 4, 2021

Disrupted protein folding or decreased stability can lead to the accumulation of (partially) un- misfolded proteins, which ultimately cause formation aggregates. Much interest in aggregation is associated with its involvement a wide range human diseases and challenges it poses for large-scale biopharmaceutical manufacturing formulation therapeutic proteins peptides. On other hand, aggregates also be functional, as observed nature, triggered use development biomaterials therapeutics well improvement food characteristics. Thus, unmasking various steps involved critical obtain better understanding underlying mechanism amyloid formation. This knowledge will allow more tailored diagnostic methods treatments amyloid-associated diseases, applications fields new (bio)materials, technology therapeutics. However, complex dynamic nature process makes study challenging. To provide guidance on how analyse aggregation, this review we summarize most commonly investigated aspects some popular corresponding methods.

Language: Английский

Citations

126
Evidence for a semisolid phase state of aerosols and droplets relevant to the airborne and surface survival of pathogens DOI Creative Commons
Erik Huynh,

Anna Olinger,

David Woolley

et al.

Proceedings of the National Academy of Sciences, Journal Year: 2022, Volume and Issue: 119(4)

Published: Jan. 21, 2022

Significance Ambient humidity can influence the survival of pathogens in respiratory aerosols and droplets, although mechanism optimum level for public health remain unclear. Here, we present evidence a humidity-dependent, semisolid state droplets relevant to pathogen survival. These observations indicate that may protect from inactivation by hindering disinfection reactions at intermediate-to-low levels. The formation was dependent on composition aerosols, which suggests destruction will depend particles released an infected host. be used help interpret laboratory studies inform recommendations.

Language: Английский

Citations

82
Derivatization with fatty acids in peptide and protein drug discovery DOI
Peter Kurtzhals, Søren Østergaard, Erica Nishimura

et al.

Nature Reviews Drug Discovery, Journal Year: 2022, Volume and Issue: 22(1), P. 59 - 80

Published: Aug. 24, 2022

Language: Английский

Citations

72
Strategies for overcoming protein and peptide instability in biodegradable drug delivery systems DOI Creative Commons
Miusi Shi, Kevin J. McHugh

Advanced Drug Delivery Reviews, Journal Year: 2023, Volume and Issue: 199, P. 114904 - 114904

Published: May 30, 2023

Language: Английский

Citations

50
The role of biomolecular condensates in protein aggregation DOI
Brent S. Visser, Wojciech P. Lipiński, Evan Spruijt

et al.

Nature Reviews Chemistry, Journal Year: 2024, Volume and Issue: 8(9), P. 686 - 700

Published: Aug. 12, 2024

Language: Английский

Citations

20
Aggregation of protein therapeutics enhances their immunogenicity: causes and mitigation strategies DOI Creative Commons
Mimmi L. E. Lundahl, Silvia Fogli, Paula E. Colavita

et al.

RSC Chemical Biology, Journal Year: 2021, Volume and Issue: 2(4), P. 1004 - 1020

Published: Jan. 1, 2021

Protein aggregation of biotherapeutics increases their immunogenicity, leading to immune-mediated adverse effects. In this review we discuss immune activation pathways, causes and mitigation strategies.

Language: Английский

Citations

97