Molecularly tuned peptideassemblies at the liquid–solid interface studied by scanning tunneling microscopy
Literature Information
Lin Niu, Xiaojing Ma, Lei Liu, Xiaobo Mao, Dongxia Wu, Yanlian Yang, Qingdao Zeng, Chen Wang
We report here the modulation of a peptide assembly with a molecular template at the liquid–solid interface using scanning tunneling microscopy (STM). A lamella structure is observed for the assembly of pentapeptide 5Ala, and the introduction of the terpyridine derivative (BT–O–C16) gives rise to co-assembled molecular architectures with pentapeptide monomers and dimers encapsulated in the nanoscale cavities of the BT–O–C16 network. The selectivity of the molecular networks could allow for programmable construction of organic–peptide architectures.
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Physical Chemistry Chemical Physics

Physical Chemistry Chemical Physics (PCCP) is an international journal co-owned by 19 physical chemistry and physics societies from around the world. This journal publishes original, cutting-edge research in physical chemistry, chemical physics and biophysical chemistry. To be suitable for publication in PCCP, articles must include significant innovation and/or insight into physical chemistry; this is the most important criterion that reviewers and Editors will judge against when evaluating submissions. The journal has a broad scope and welcomes contributions spanning experiment, theory, computation and data science. Topical coverage includes spectroscopy, dynamics, kinetics, statistical mechanics, thermodynamics, electrochemistry, catalysis, surface science, quantum mechanics, quantum computing and machine learning. Interdisciplinary research areas such as polymers and soft matter, materials, nanoscience, energy, surfaces/interfaces, and biophysical chemistry are welcomed if they demonstrate significant innovation and/or insight into physical chemistry. Joined experimental/theoretical studies are particularly appreciated when complementary and based on up-to-date approaches.











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