Quarterly Reviews of Biophysics最新文献

The pivotal roles of cellular biophysics and mechanobiology in the development of Human Organs-on-Chips. 细胞生物物理学和机械生物学在人体器官芯片发展中的关键作用。

IF 5.3 2区生物学

Quarterly Reviews of Biophysics Pub Date : 2026-05-04 DOI: 10.1017/S003358352610016X

Donald E Ingber

{"title":"The pivotal roles of cellular biophysics and mechanobiology in the development of Human Organs-on-Chips.","authors":"Donald E Ingber","doi":"10.1017/S003358352610016X","DOIUrl":"https://doi.org/10.1017/S003358352610016X","url":null,"abstract":"The development of Human Organs-on-Chips (Organ Chips) - microfluidic culture devices lined by living human tissues that recapitulate organ-level pathophysiology and offer a new approach to replace animal testing in drug development and advance personalized medicine - is often viewed through the lens of bioengineering and microfabrication. However, the origin of this technology lies deeply rooted in pursuit of a fundamental understanding of cellular biophysics and human mechanobiology. This review is written primarily from a personal perspective, and it traces work beginning 50 years ago, which describes how the need for new experimental tools to test a novel tensegrity model of cellular mechanics and mechanotransduction led to the melding of cell biology, engineering, and computer microchip manufacturing approaches, and eventually to the birth of Organ Chip technology. The initial driving force was the need to artificially control the shape of living cells to demonstrate the central role that mechanical forces play in biological control. This led to the adoption of soft lithography to create tailored cell culture environments and later to the development of mechanically active, microfluidic Organ Chip culture systems. By recapitulating tissue-tissue interfaces and the dynamic mechanical microenvironments of living organs, Organ Chips enable understanding of mechanobiological phenomena that are unattainable with traditional static cell cultures or animal models. This path of research has confirmed the indispensable importance of physical forces for physiological control, in addition to accelerating drug discovery, enhancing toxicity assessment, and deepening our comprehension of disease pathogenesis.","PeriodicalId":20828,"journal":{"name":"Quarterly Reviews of Biophysics","volume":"59 ","pages":"e9"},"PeriodicalIF":5.3,"publicationDate":"2026-05-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147820097","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Biophysics meets fungal biology: Characterising the fungal cell envelope and its interactions with drug-like molecules. 生物物理学与真菌生物学：表征真菌细胞包膜及其与药物样分子的相互作用。

IF 5.3 2区生物学

Quarterly Reviews of Biophysics Pub Date : 2026-04-28 DOI: 10.1017/S0033583526100158

Obed Obeng-Gyasi, Evelyne Deplazes

{"title":"Biophysics meets fungal biology: Characterising the fungal cell envelope and its interactions with drug-like molecules.","authors":"Obed Obeng-Gyasi, Evelyne Deplazes","doi":"10.1017/S0033583526100158","DOIUrl":"https://doi.org/10.1017/S0033583526100158","url":null,"abstract":"The fungal cell envelope, consisting of the cell wall and plasma membrane, is a dynamic structure crucial for cell shape, viability, pathogenicity, and the cell's ability to interact with and respond to its environment. Most antifungal drug development target components of the fungal plasma membrane and cell wall, thus understanding its composition and interactions with small molecules is vital for biomedical research and drug development. However, studying cell walls and membranes is challenging due to their high degree of complexity, their heterogeneous and dynamic structure and their sensitivity to environmental conditions. Our review provides a unique exploration of how biophysical techniques have advanced our understanding of the cell envelope's structure, its role in fungal pathogenicity, and drug resistance, which are critical issues for global health and food security. We highlight recent advances in microscopy and spectroscopy approaches, combined with analytical techniques and lipidomics, that have enabled detailed study of fungal cell walls and plasma membranes at unprecedented spatial and temporal resolutions. These studies have helped provide structural models of fungal cell walls and plasma membranes, including important differences between clinically relevant fungal species that are critical for antifungal drug development. Our review also summarises commonly used model membranes systems and discusses challenges and considerations in bridging gaps between simplified models and cellular systems, and why they are lacking compared to bacterial and mammalian systems and what is required to improve these systems.","PeriodicalId":20828,"journal":{"name":"Quarterly Reviews of Biophysics","volume":"59 ","pages":"e8"},"PeriodicalIF":5.3,"publicationDate":"2026-04-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147779500","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Energy landscapes in molecular biology: History, principles, and perspectives. 分子生物学中的能量景观：历史、原理和观点。

IF 5.3 2区生物学

Quarterly Reviews of Biophysics Pub Date : 2026-04-22 DOI: 10.1017/S0033583526100134

Ruth Nussinov, Clil Regev, Hyunbum Jang

{"title":"Energy landscapes in molecular biology: History, principles, and perspectives.","authors":"Ruth Nussinov, Clil Regev, Hyunbum Jang","doi":"10.1017/S0033583526100134","DOIUrl":"https://doi.org/10.1017/S0033583526100134","url":null,"abstract":"In an editorial for a Special Issue, Nussinov and Wolynes explored the energy landscapes of biomolecular function, questioning whether they constituted a second molecular biology revolution. With more than a decade having passed and science having progressed significantly, we revisit this question. Statistical energy landscapes not only visualize folding funnels but also quantify the likelihoods of different states, embodying the foundational physical-chemical principles of protein actions. Building upon the theory of energy landscapes, the conformational selection and population shift paradigm posited that since all functional conformations already pre-exist in a dynamic equilibrium, a ligand 'selects' and stabilizes a state from this pre-existing pool, resulting in re-equilibration, or shift, of the population. The principle that it established - that function harnesses transitions between pre-existing conformations - revolutionized the understanding of allostery and, broadly, regulation. This paradigm challenged and superseded the decades-old, albeit persisting, belief of only one (or two; 'open' and 'closed') protein conformations. It also indicates that for engineered proteins to exert effective function, we must account for the timescales of flipping between energy landscape states, for example, by tuning the barrier heights. Returning to the question of whether landscapes constituted a second biomolecular biology revolution, we consider their bedrock contributions, which are far beyond the original protein folding funnels. They established the principle of multiple dynamic conformational states 'jumping' over barriers during population shifts. By leveraging core concepts like conformational ensembles, modern molecular biology has achieved breakthroughs such as next-generation allosteric drugs, indeed leading to a transformative era in molecular science.","PeriodicalId":20828,"journal":{"name":"Quarterly Reviews of Biophysics","volume":"59 ","pages":"e7"},"PeriodicalIF":5.3,"publicationDate":"2026-04-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147779503","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The influence of structure, dissociation constants, and an aqueous environment on the physicochemical properties of L-α-amino acids. 结构、解离常数和水环境对L-α-氨基酸理化性质的影响。

IF 5.3 2区生物学

Quarterly Reviews of Biophysics Pub Date : 2026-04-07 DOI: 10.1017/S0033583526100146

Marek Pająk, Magdalena Woźniczka, Elżbieta Kamysz, Marcin Banach, Jakub Fichna

{"title":"The influence of structure, dissociation constants, and an aqueous environment on the physicochemical properties of L-α-amino acids.","authors":"Marek Pająk, Magdalena Woźniczka, Elżbieta Kamysz, Marcin Banach, Jakub Fichna","doi":"10.1017/S0033583526100146","DOIUrl":"https://doi.org/10.1017/S0033583526100146","url":null,"abstract":"L-α-amino acids are the fundamental building blocks of proteins and play a pivotal role in the biochemistry of living organisms. The behavior of these molecules in an aqueous solution – the primary medium for biological reactions – is contingent on their physicochemical properties, including molecular structure and dissociation constants (Ka). The objective of this article is to provide a comprehensive description of the chemical significance of amino acids in an aqueous environment. This encompasses their ionization states at varying pH, interactions with water molecules, environmental effects (e.g., ionic strength, temperature, the presence of other ions, and pressure), and the implications of these factors for the stability and biological function of the example peptides and proteins. The article also presents a discussion of contemporary experimental and computational methodologies employed in the study of the physicochemical properties of amino acids in an aqueous solution. It is imperative that these relationships are comprehended if advancements in the fields of drug design, protein engineering, and biotechnology are to be facilitated.","PeriodicalId":20828,"journal":{"name":"Quarterly Reviews of Biophysics","volume":"59 ","pages":"e6"},"PeriodicalIF":5.3,"publicationDate":"2026-04-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147628299","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Crystallographic binding modes of octahedral transition metal complexes to duplex DNA. 八面体过渡金属配合物与双链DNA的结晶结合模式。

IF 5.3 2区生物学

Quarterly Reviews of Biophysics Pub Date : 2026-03-30 DOI: 10.1017/S0033583526100122

Tayler D Prieto Otoya, Christine Janet Cardin

引用次数: 0

Cryo-EM of endogenous membrane proteins in their native lipid bilayer. 内源性膜蛋白在其天然脂质双分子层中的低温电镜观察。

IF 5.3 2区生物学

Quarterly Reviews of Biophysics Pub Date : 2026-03-06 DOI: 10.1017/S0033583526100109

John L Rubinstein

引用次数: 0

Revealing protein dynamics with high-pressure NMR. 用高压核磁共振揭示蛋白质动力学。

IF 5.3 2区生物学

Quarterly Reviews of Biophysics Pub Date : 2026-02-26 DOI: 10.1017/S0033583526100092

Julien Roche, Christian Roumestand, Catherine A Royer

引用次数: 0

The energy barrier model in membrane biophysics: Ion flow, current-voltage relations, and Donnan osmosis. 膜生物物理学中的能量势垒模型：离子流、电流-电压关系和唐南渗透。

IF 5.3 2区生物学

Quarterly Reviews of Biophysics Pub Date : 2026-02-25 DOI: 10.1017/S0033583526100110

Gerald Manning

{"title":"The energy barrier model in membrane biophysics: Ion flow, current-voltage relations, and Donnan osmosis.","authors":"Gerald Manning","doi":"10.1017/S0033583526100110","DOIUrl":"10.1017/S0033583526100110","url":null,"abstract":"Theoretical analysis of an energy barrier model for the electrical properties of a biological membrane yields new results. Discontinuities at the membrane-solution interfaces are crucial and receive careful attention, as does the polarization charge density due to electroneutral but polarized ion distributions. The topics explored include the equilibrium and time-dependent Nernst potential, the resting potential, the capacitance-resistance equation for membrane voltage, and large electrical effects on osmosis (bulk volume flow). The generalization of Nernst-Hartley salt diffusion to the diffusion of mixed salts as a necessary tool is accomplished. The electric field inside the membrane is especially strong at the membrane-solution interfaces. The analysis of the resting potential differs from the Goldman-Hodgkin-Katz formulation but predicts realistic numerical values for animal cells and also captures the effect of switching sodium and potassium ion permeabilities. An analysis of the physical basis of bulk water flow in the presence of impermeant and permeant ions, that is, Donnan osmosis, reveals large ion charge effects that have not previously been considered. The equation derived here for Donnan osmotic flow helps to explain why the action of the sodium pump is essential for the prevention of excessive osmotic stress on cellular membranes.","PeriodicalId":20828,"journal":{"name":"Quarterly Reviews of Biophysics","volume":"59 ","pages":"e1"},"PeriodicalIF":5.3,"publicationDate":"2026-02-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147284876","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The multifaceted character of water as solvent for proteins: From poor for folded proteins to good for (some) intrinsically disordered proteins and protein segments. 水作为蛋白质溶剂的多面性：从对折叠蛋白质的不利到对（某些）内在无序的蛋白质和蛋白质片段的有利。

IF 5.3 2区生物学

Quarterly Reviews of Biophysics Pub Date : 2026-02-23 DOI: 10.1017/S0033583526100080

Reinhard Schweitzer-Stenner

{"title":"The multifaceted character of water as solvent for proteins: From poor for folded proteins to good for (some) intrinsically disordered proteins and protein segments.","authors":"Reinhard Schweitzer-Stenner","doi":"10.1017/S0033583526100080","DOIUrl":"10.1017/S0033583526100080","url":null,"abstract":"Intrinsically disordered proteins (IDPs) and disordered regions of folded proteins (IDRs) perform a plethora of cellular functions involving interactions with a variety of proteins, DNA, and RNA. Their flexibility enables them to interact with different cellular components. They can adopt molten globule as well as extended statistical coil structures depending on their amino acid residue sequence. They are generally more enriched in polar and charged residues, which generally facilitate solvation. This review article asks to what extent water as a solvent affects local (on a residue level) and global properties (size, Flory exponents) of IDPs. It introduces various aspects of protein hydration in the folded state as a benchmark and reference. The results of experimental and computational studies on short model peptides reveal how local structural propensities of residues are determined by water-backbone and water-side chain interactions. Ramachandran plots of individual amino acid residues are side-chain and neighbor-dependent. For unfolded oligo-peptides and IDPs (IDRs) the article discusses the intricated relationship between IDP hydration and global parameters (i.e., radius of gyration), which involves multiple parameters such as net charge, charge distribution, hydrophobicity, and the ionic strength of the aqueous solution. A review of experimental work that explored the strength of water-protein interactions and their influence on water dynamics reveals significant differences between water binding to folded and disordered proteins. Finally, The role of water in liquid-liquid mixing of short peptides and IDPs is delineated, which can lead to gelation and the formation of membrane-less droplets.","PeriodicalId":20828,"journal":{"name":"Quarterly Reviews of Biophysics","volume":" ","pages":"e5"},"PeriodicalIF":5.3,"publicationDate":"2026-02-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147271882","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Delivery of macromolecular drugs: An update. 大分子药物的递送：最新进展。

IF 5.3 2区生物学

Quarterly Reviews of Biophysics Pub Date : 2025-11-18 DOI: 10.1017/S0033583525100073

Robert Langer

引用次数: 0