Jian R. Lu

East China Normal University

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Hai Xu

China University of Petroleum, East China

101

Xiubo Zhao

Changzhou University

Robert K. Thomas

University of Oxford

Xuzhi Hu

University of Manchester

Fang Pan

Xi'an Jiaotong University

Zongyi Li

University of Manchester

Jiqian Wang

China University of Petroleum, East China

Thomas Andrew Waigh

University of Manchester

J. Penfold

Rutherford Appleton Laboratory

Mingrui Liao

University of Manchester

Cooperative Institutions

University of Manchester

155

Chinese Academy of Sciences

117

China University of Petroleum, East China

113

Rutherford Appleton Laboratory

University of Chinese Academy of Sciences

Shanghai Jiao Tong University

University of Oxford

Zhejiang University

China University of Petroleum, Beijing

Sun Yat-sen University

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Intramembrane Nanoaggregates of Antimicrobial Peptides Play a Vital Role in Bacterial Killing

Small (2022)

Mingrui Liao Haoning Gong Xuebo Quan Ziwei Wang Xuzhi Hu

Abstract Recent developments in antimicrobial peptides (AMPs) have focused on the rational design of short sequences with less than 20 amino acids due to their relatively low synthesis costs and ease of correlation of the structure‐function relationship. However, gaps remain in the understanding of how short cationic AMPs interact with the bacterial outer and inner membranes to affect their antimicrobial efficacy and dynamic killing. The membrane‐lytic actions of two designed AMPs, G(IIKK) 3 I‐NH 2 (G 3 ) and G(IIKK) 4 I‐NH 2 (G 4 ), and previously‐studied controls GLLDLLKLLLKAAG‐NH 2 (LDKA, biomimetic) and GIGAVLKVLTTGLPALISWIKRKR‐NH 2 (Melittin, natural) are examined. The mechanistic processes of membrane damage and the disruption strength of the four AMPs are characterized by molecular dynamics simulations and experimental measurements including neutron reflection and scattering. The results from the combined studies are characterized with distinctly different intramembrane nanoaggregates formed upon AMP‐specific binding, reflecting clear influences of AMP sequence, charge and the chemistry of the inner and outer membranes. G 3 and G 4 display different nanoaggregation with the outer and inner membranes, and the smaller sizes and further extent of insertion of the intramembrane nanoaggregates into bacterial membranes correlate well with their greater antimicrobial efficacy and faster dynamic killing. This work demonstrates the crucial roles of intramembrane nanoaggregates in optimizing antimicrobial efficacy and dynamic killing.

Melittin

Inner membrane

Lytic cycle

Rational design

10.1002/smll.202204428

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Citations (19)

Optimizing CsPbBr3 perovskite solar cell interface and performance through tetraphenylethene derivatives

Chinese Chemical Letters (2025)

Sheng Tang Mingyue Liao Wen‐Hua Sun Jihuai Wu Jian R. Lu

Interface (matter)

10.1016/j.cclet.2025.110838

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Citations (0)

Recent development of peptide self-assembly

Progress in Natural Science Materials International (2008)

Xiubo Zhao Fang Pan Jian R. Lu

Amino acids are the building blocks to build peptides and proteins. Recent development in peptide synthesis has however enabled us to mimic this natural process by preparing various long and short peptides possessing different conformations and biological functions. The self-assembly of short designed peptides into molecular nanostructures is becoming a growing interest in nanobiotechnology. Self-assembled peptides exhibit several attractive features for applications in tissue regeneration, drug delivery, biological surface engineering as well as in food science, cosmetic industry and antibiotics. The aim of this review is to introduce the readers to a number of representative studies on peptide self-assembly.

Nanobiotechnology

10.1016/j.pnsc.2008.01.012

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Citations (77)

Dynamic adsorption of monoclonal antibody layers on hydrophilic silica surface: A combined study by spectroscopic ellipsometry and AFM

Journal of Colloid and Interface Science (2008)

Xiaoqiang Wang Yuming Wang Hai Xu Honghong Shan Jian R. Lu

Ellipsometry

10.1016/j.jcis.2008.04.024

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Citations (66)

Analysis of a degron-containing reporter protein GFP-CL1 reveals a role for SUMO1 in cytosolic protein quality control

Journal of Biological Chemistry (2022)

Wei Wang Jian R. Lu Wei-Chih Yang Eric D. Spear Susan Michaelis

Degron

Proteostasis

Protein Degradation

AAA proteins

10.1016/j.jbc.2022.102851

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Citations (5)

Formation and identification of trimethylimidazole during tetramethylpyrazine production from glucose by Bacillus strains

Biotechnology Letters (2009)

Zijun Xiao Jian R. Lu Cuiqing Ma Ping Xu

Tetramethylpyrazine

Bacillus (shape)

10.1007/s10529-009-0012-7

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Citations (5)

Neutron reflection and scattering in characterising peptide assemblies

Advances in Colloid and Interface Science (2023)

Xuzhi Hu Mingrui Liao Ke Ding Jiqian Wang Hai Xu

Self-assemblies of de novo designed short peptides at interface and in bulk solution provide potential platforms for developing applications in many medical and technological areas. However, characterising how bioinspired supramolecular nanostructures evolve with dynamic self-assembling processes and respond to different stimuli remains challenging. Neutron scattering technologies including small angle neutron scattering (SANS) and neutron reflection (NR) can be advantageous and complementary to other state-of-the-art techniques in tracing structural changes under different conditions. With more neutron sources now available, SANS and NR are becoming increasingly popular in studying self-assembling processes of diverse peptide and protein systems, but the difficulty in experimental manipulation and data analysis can deter beginners. This review will introduce the basic theory, general experimental setup and data analysis of SANS and NR, followed by provision of their applications in characterising interfacial and solution self-assemblies of representative peptides and proteins. SANS and NR are remarkably effective in determining the morphological features self-assembled short peptides, especially size and shape transitions as a result of either sequence changes or in response to environmental stimuli, demonstrating the unique capability of NR and SANS in unravelling the interactive processes. These examples highlight the potential of NR and SANS in supporting the development of novel short peptides and proteins as biopharmaceutical candidates in the fight against many diseases and infections that share common features of membrane interactive processes.

Reflection

10.1016/j.cis.2023.103033

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Citations (5)

Influence of Molecular Structure on the Size, Shape, and Nanostructure of Nonionic C_nE_m Surfactant Micelles

The Journal of Physical Chemistry B (2013)

Faheem Padia Mohammed Yaseen Barbara Gore Sarah E. Rogers Gordon Bell

Nonionic alkyl ethoxylates (CnEm) have been extensively studied for their adsorption, aggregation, and solubilization individually and in small groups. In this work, we report a more systematic study of the effects of alkyl chain (tail) and ethoxylate (head) length on the size, shape, and extent of intermixing within the CnEm micelles in aqueous solution. Data from small angle neutron scattering (SANS) and nuclear magnetic resonance (NMR) were combined to undertake the structural characterization of micelles formed from the two separate series of surfactants CnE6 (n = 10, 12, 14) and C12Em (m = 5, 6, 8, 10, 12). The micellar core volume (Vcore) could be well determined with reasonable accuracy and linked to the hydrophilic–lipophilic balance (HLB) of the surfactant, with a sharp size and shape transition occurring around HLB = 12.5. NOESY NMR results revealed protrusions of the terminal methylene groups into the ethoxylate shell, thus providing direct experimental evidence for the phenomenon of "roughness" or intermixing of the core–shell interface. These detailed studies are compared with previous investigations on this model surfactant system.

Methylene

10.1021/jp409808c

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Citations (37)

Coadsorption of Human Milk Lactoferrin into the Dipalmitoylglycerolphosphatidylcholine Phospholipid Monolayer Spread at the Air/Water Interface

Biophysical Journal (2006)

Fausto Miano Xiubo Zhao Jian R. Lu J. Penfold

Lactoferrin

Surface pressure

X-ray reflectivity

Neutron reflectometry

10.1529/biophysj.105.078592