TY - JOUR

T1 - Piezoactive Bioorganic Diphenylalanine Films: Mechanism of Phase Formation

AU - Alikin, Denis

AU - Yuzhakov, Vladimir

AU - Semiletova, Larisa

AU - Slabov, Vladislav

AU - Kuznetsov, Dmitrii

AU - Gimadeeva, Lubov

AU - Shur, Vladimir

AU - Kopyl, Svetlana A.

AU - Kholkin, Andrei

N1 - Текст о финансировании #1 The research funding from the Ministry of Science and Higher Education of the Russian Federation (Ural Federal University Program of Development within the Priority-2030 Program) is acknowledged. Текст о финансировании #2 The research funding from the Ministry of Science and Higher Education of the Russian Federation (Ural Federal University Program of Development within the Priority-2030 Program) is gratefully acknowledged. The equipment of the Ural Center for Shared Use “Modern nanotechnology” of Ural Federal University (reg. # 2968) was used. The authors acknowledge Boris Slautin for help with the neuro-net setup. The research funding from the Ministry of Science and Higher Education of the Russian Federation (Ural Federal University Program of Development within the Priority-2030 Program) is acknowledged.

PY - 2023

Y1 - 2023

N2 - Self-organized peptides are unique materials with various applications in biology, medicine, and nanotechnology. Many of these applications require fabrication of homogeneous thin films having high piezoelectric effect and sufficiently low roughness. Recently, a facile method for the controlled deposition of flat solid films of the most studied peptide, diphenylalanine (FF), has been proposed, which is based on the crystallization of FF in the amorphous phase under the action of water vapor. This method is very advantageous compared with crystallization from a liquid phase reported previously. Here, we thoroughly investigate the mechanism of solid-state transformation from the amorphous to crystalline phase. The study revealed that the process proceeds in two distinct stages, maintaining clamped condition of self-assembling building blocks that preserve the films’ morphology and high piezoelectric activity. We emphasize the critical role of water diffusion that governs two-dimensional growth of crystalline domains in FF films, merging in very dense, flat, and homogeneous films. These findings open a wide perspective for using this methodology for the direct fabrication of biofilms from the amorphous phase. We thus expect the application of these films to various nanotechnological applications of self-assembled structures. © 2023 American Chemical Society.

AB - Self-organized peptides are unique materials with various applications in biology, medicine, and nanotechnology. Many of these applications require fabrication of homogeneous thin films having high piezoelectric effect and sufficiently low roughness. Recently, a facile method for the controlled deposition of flat solid films of the most studied peptide, diphenylalanine (FF), has been proposed, which is based on the crystallization of FF in the amorphous phase under the action of water vapor. This method is very advantageous compared with crystallization from a liquid phase reported previously. Here, we thoroughly investigate the mechanism of solid-state transformation from the amorphous to crystalline phase. The study revealed that the process proceeds in two distinct stages, maintaining clamped condition of self-assembling building blocks that preserve the films’ morphology and high piezoelectric activity. We emphasize the critical role of water diffusion that governs two-dimensional growth of crystalline domains in FF films, merging in very dense, flat, and homogeneous films. These findings open a wide perspective for using this methodology for the direct fabrication of biofilms from the amorphous phase. We thus expect the application of these films to various nanotechnological applications of self-assembled structures. © 2023 American Chemical Society.

UR - http://www.scopus.com/inward/record.url?partnerID=8YFLogxK&scp=85179813955

UR - https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=tsmetrics&SrcApp=tsm_test&DestApp=WOS_CPL&DestLinkType=FullRecord&KeyUT=001123859800001

U2 - 10.1021/acsbiomaterials.3c01507

DO - 10.1021/acsbiomaterials.3c01507

M3 - Article

VL - 9

SP - 6715

EP - 6723

JO - ACS Biomaterials Science and Engineering

JF - ACS Biomaterials Science and Engineering

SN - 2373-9878

IS - 12

ER -