Article
Biochemistry & Molecular Biology
Lucia De Rosa, Donatella Diana, Domenica Capasso, Rachele Stefania, Rossella Di Stasi, Roberto Fattorusso, Luca Domenico D'Andrea
Summary: In this study, we investigated the impact of chiral inversion of the N-capping sequence on the folding of the VEGF mimetic helical peptide QK, and evaluated its effect on stability and biological activity through experiments.
Article
Biology
Philippe Karoyan, Vincent Vieillard, Luis Gomez-Morales, Estelle Odile, Amelie Guihot, Charles-Edouard Luyt, Alexis Denis, Pascal Grondin, Olivier Lequin
Summary: The researchers developed peptide mimics based on the N-terminal helix of hACE2 protein to block SARS-CoV-2 infection, showing potential for prophylactic and therapeutic use in combating COVID-19.
COMMUNICATIONS BIOLOGY
(2021)
Article
Biochemistry & Molecular Biology
Violeta Markovic, Jeelan Basha Shaik, Katarzyna Ozga, Agnieszka Ciesiolkiewicz, Juan Lizandra Perez, Ewa Rudzinska-Szostak, Lukasz Berlicki
Summary: The entry of the SARS-CoV-2 virus into a human host cell begins with the interaction between the viral spike protein (S protein) and human angiotensin-converting enzyme 2 (hACE2). A possible strategy for the treatment of this infection is based on inhibiting the interaction of the two abovementioned proteins.
JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
(2023)
Article
Chemistry, Multidisciplinary
Giulia Marafon, Marco Crisma, Anna Masato, Nicoletta Plotegher, Luigi Bubacco, Alessandro Moretto
Summary: Proteins undergo changes in their 3D structure and function through specific molecular interactions, which is crucial for sensing, processing, and transmitting information from the surrounding environment. The study of early aggregation steps of alpha-synuclein associated with Parkinson's disease showed that light-mediated binding with a photoactive foldamer can promote the process by generating supramolecular fibrillar seeds that act as molecular templates for inducing fast beta-sheet transitions in monomers. This proposed method provides a powerful tool for studying protein aggregation in misfolding diseases in a controlled and inducible system.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
(2021)
Article
Biochemistry & Molecular Biology
Irena Roterman, Katarzyna Stapor, Dawid Dulak, Leszek Konieczny
Summary: The experimentally determined structures of amyloid forms are primarily characterized by the two-dimensional forms of a single polypeptide chain, which is made possible by the beta structure and the numerous hydrogen bonds. This study proposes a possible mechanism for obtaining such a structure based on the geometric characterization of the polypeptide chain and molecular dynamics results. The potential mechanism of amyloid transformation is presented using transthyretin and amyloid A beta as examples.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2022)
Review
Chemistry, Medicinal
Sergio Algar, Mercedes Martin-Martinez, Rosario Gonzalez-Muniz
Summary: Researchers have developed a variety of non-peptide alpha-helix mimetics to modulate protein-protein interactions, with the potential to stabilize or disrupt therapeutically relevant PPIs. The diverse chemical structures and substituents allow for a wide range of choices in research, offering new opportunities for future studies on protein interactions.
EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY
(2021)
Article
Chemistry, Multidisciplinary
Sebastian Dengler, Pradeep K. Mandal, Lars Allmendinger, Celine Douat, Ivan Huc
Summary: Incorporating an aromatic foldamer segment into a macrocyclic peptide can influence its conformation and properties. The study reveals that the foldamer helical folding tends to prevail and stretch peptides in a solvent-dependent manner, while peptides also reciprocally affect foldamer helix handedness bias and stabilization. The hybrid macrocycles exhibit resistance towards proteolytic degradation.
Article
Multidisciplinary Sciences
Kobe Janssen, Filip Claes, Dido Van de Velde, Vanessa L. Wehbi, Bert Houben, Yulia Lampi, Mieke Nys, Laleh Khodaparast, Ladan Khodaparast, Nikolaos Louros, Rob van der Kant, Joffre Verniers, Teresa Garcia, Meine Ramakers, Katerina Konstantoulea, Katerina Maragkou, Ramon Duran-Romana, Monica Musteanu, Mariano Barbacid, Bernard Scorneaux, Els Beirnaert, Joost Schymkowitz, Frederic Rousseau
Summary: Mutant KRAS is a challenging target for classical small molecule drugs, but this study shows that its misfolding can be induced by synthetic peptides derived from specific regions of the oncoprotein. These peptides were able to inhibit the function of mutant KRAS and showed antiproliferative activity against cancer cells. The findings provide proof-of-concept for exploiting the intrinsic misfolding propensity of KRAS as a therapeutic strategy.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(2023)
Review
Biochemistry & Molecular Biology
Karolina Corin, James U. Bowie
Summary: Protein folding is a crucial process in life, and mutations associated with diseases are believed to primarily affect folding rather than function. Studying membrane protein folding is more difficult than soluble proteins due to complex folding environments. However, advancements in experimental techniques and model systems are helping unravel the forces and pathways involved in membrane protein folding.
Article
Chemistry, Multidisciplinary
Jean-Francois Gaucher, Marie Reille-Seroussi, Sylvain Broussy
Summary: This study investigates the effects of macrocyclization constraints on peptide ligands, showing that differences in thermodynamics come mainly from the folding energy of the peptide upon binding. The reduction in conformational entropy penalty due to helix pre-organization can be counterbalanced by an unfavorable vibrational entropy change if the constraints are too rigid. The gain in configurational entropy partially escapes the enthalpy/entropy compensation and leads to an improvement in affinity.
CHEMISTRY-A EUROPEAN JOURNAL
(2022)
Article
Cell Biology
Anton A. Komar
Summary: Protein folding in the cell is largely co-translational, occurring during protein synthesis on the ribosome. It has been found that co-translational folding is characteristic of almost all types of proteins in the cell, including single and multidomain, single and multisubunit, cytosolic, secretory, and membrane proteins. However, many details of co-translational folding are still not fully understood. Recent research has shown that folding of a beta-barrel protein begins with the formation of an alpha-helix inside the ribosome, which then rearranges into a beta-hairpin structure as the peptide grows and reaches the wider region of the ribosomal exit tunnel.
Article
Chemistry, Organic
Lydia Zengerling, Benedict Kemper, Ute A. Hellmich, Pol Besenius
Summary: The synthesis of hexa- and dodecapeptides functionalized with two Au(I)-phosphine complexes is reported. The high stability of the Au(I)-phosphine bond allowed orthogonal peptide-protecting group chemistry, resulting in metallododecapeptides with α-helical secondary structures of high thermal stability in specific solvent mixtures.
Article
Biochemistry & Molecular Biology
Sunit Pal, Shreya Banerjee, Erode N. Prabhakaran
Summary: The resistance of helical folds to thermal perturbations is related to the similarity between the nucleating and propagating segments, with the folding process influenced by the template provided by the nucleating segment.
Article
Engineering, Environmental
Rui Liu, Haozheng Wang, Wenjun Lu, Lei Cui, Sha Wang, Yafei Wang, Qianbing Chen, Ying Guan, Yongjun Zhang
Summary: By introducing helical peptide chains into hydrogel networks using peptide crosslinkers, the synthetic hydrogels achieve significantly improved mechanical strength and extensibility, solving the dilemma of designing a gel with both high toughness and resilience.
CHEMICAL ENGINEERING JOURNAL
(2021)
Article
Chemistry, Physical
Wenbo Zhang, Mingwei Liu, Lanlan Yu, Shanshan Mo, Zhun Deng, Shuli Liu, Yanlian Yang, Chen Wang, Chenxuan Wang
Summary: This study demonstrates the contribution of various noncovalent interactions to supramolecular assembly by investigating the self-assembly of peptides.
JOURNAL OF COLLOID AND INTERFACE SCIENCE
(2022)
Article
Biochemistry & Molecular Biology
Valerie T. Ressler, Ronald T. Raines
Editorial Material
Biochemical Research Methods
Theresa M. Reineke, Ronald T. Raines, Vincent M. Rotello
BIOCONJUGATE CHEMISTRY
(2019)
Article
Biochemistry & Molecular Biology
Ian W. Windsor, Crystal J. Graff, Ronald T. Raines
Article
Biochemistry & Molecular Biology
Aubrey J. Ellison, I. Caglar Tanrikulu, Jesus M. Dones, Ronald T. Raines
Article
Biology
Lindsey R. F. Backman, Yolanda Y. Huang, Mary C. Andorfer, Brian Gold, Ronald T. Raines, Emily P. Balskus, Catherine L. Drennan
Article
Biochemistry & Molecular Biology
Henry R. Kilgore, Andrew P. Latham, Valerie T. Ressler, Bin Zhang, Ronald T. Raines
Article
Biochemistry & Molecular Biology
Nile S. Abularrage, Brian J. Levandowski, Ronald T. Raines
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2020)
Article
Chemistry, Medicinal
Chelcie H. Eller, Ronald T. Raines
ACS INFECTIOUS DISEASES
(2020)
Article
Biochemical Research Methods
Jessica Sayers, Evans C. Wralstad, Ronald T. Raines
Summary: The ribonuclease S complex has led to historic discoveries in protein chemistry and enzymology, but its applications have been hindered by two main drawbacks: immune response in humans and susceptibility to dissociation. By semi-synthesizing an RNase S conjugate derived from human pancreatic ribonuclease and stabilized with a covalent interfragment cross-link, these limitations have been addressed, enabling unprecedented applications of the RNase-S system.
BIOCONJUGATE CHEMISTRY
(2021)
Article
Biochemistry & Molecular Biology
Sayani Chattopadhyay, Leandro B. C. Teixeira, Laura L. Kiessling, Jonathan F. McAnulty, Ronald T. Raines
Summary: This study provides a method to upregulate the TGF-beta signaling pathway by clustering the extracellular domains of TGF-beta receptors, which can enhance wound healing.
ACS CHEMICAL BIOLOGY
(2022)
Review
Biochemistry & Molecular Biology
Emily R. Garnett, Ronald T. Raines
Summary: Pancreatic-type ribonucleases (ptRNases) are a family of vertebrate-specific secretory endoribonucleases that catalyze the degradation of RNA substrates and mediate biological functions. Two ptRNases, RNase 1 and angiogenin, are known to be involved in inflammation, blood coagulation, neovascularization, cancer, amyotrophic lateral sclerosis, and cellular stress response. Further research is ongoing to elucidate the biology of these and other ptRNases.
CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY
(2022)
Article
Infectious Diseases
Ian W. Windsor, Dawn M. Dudley, David H. O'Connor, Ronald T. Raines
Summary: By engineering amino acid substitutions in RNase 1, it has been transformed into a zymogen that can be activated by HIV-1 protease, showing high toxicity towards infected cells.
AIDS RESEARCH AND THERAPY
(2021)
Article
Biochemistry & Molecular Biology
Linus B. Boll, Ronald T. Raines
Summary: The position of Cys in a protein sequence can be exploited to improve site-selectivity in maleimide-based modifications, while differences in the reactivity of Lys towards an NHS ester are modest.
Meeting Abstract
Biochemistry & Molecular Biology
Lindsey R. F. Backman, Yolanda Y. Huang, Mary C. Andorfer, Brian Gold, Ronald T. Raines, Emily P. Balskus, Catherine L. Drennan
Meeting Abstract
Biochemistry & Molecular Biology
Henry Ralph Kilgore, Valerie T. Ressler, Ronald T. Raines