A.S. Morozova a*, E.O. Kudryavtseva a,b**,

S.A. Ziganshina a,b***, M.A. Ziganshin b****A.A. Bukharaev a*****

aZavoisky Physical-Technical Institute, FRC Kazan Scientific Center,

Russian Academy of Sciences, Kazan, 420029 Russia

bKazan Federal University, Kazan, 420008 Russia

E-mail: *morozova_anna_s@mail.ru, **justqu1@yandex.ru, ***sufia@knc.ru,

****Marat.Ziganshin@kpfu.ru, *****a_bukharaev@mail.ru

Received December 26, 2022; Accepted February 6, 2023

 

ORIGINAL ARTICLE

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DOI: 10.26907/2542-064X.2023.1.37-48

For citation: Morozova A.S., Kudryavtseva E.O., Ziganshina S.A., Ziganshin M.A., Bukharaev A.A. Self-assembly of the dipeptide L-alanyl-L-phenylalanine under the action of methanol vapor with the formation of micro- and nanostructures. Uchenye Zapiski Kazanskogo Universiteta. Seriya Estestvennye Nauki, 2023, vol. 165, no. 1, pp. 37–48. doi: 10.26907/2542-064X.2023.1.37-48. (In Russian)

 

Abstract

The mechanism of self-assembly by short-chain peptides (oligopeptides) – the process by which their molecules spontaneously form an ordered structure – has received much attention recently. Self-assembling phenylalanine oligopeptides have been of particular interest due to their potential as an effective aid in the design of new functional materials. This paper considers the results of an SPM study on the ability of L-alanyl-L-phenylalanine to self-assemble into a thin film under the action of methanol vapor. The micro- and nanostructures that develop on the surface of amorphous films of this dipeptide were characterized. A method for monitoring the state of the surface of dipeptide films using atomic force spectroscopy was proposed. The results obtained contribute to the development of approaches for the controlled self-assembly of oligopeptides used to produce new biocompatible materials and environmentally friendly micro- and nanodevices that would help solve various problems in the medical, environmental, and energy fields.

Keywords: dipeptides, self-assembly, thin films, microstructures, nanostructures, atomic force microscopy

Acknowledgements. This study was performed under the state assignment to the FRC Kazan Scientific Center, Russian Academy of Sciences (A.S. Morozova, E.O. Kudryavtseva, A.A. Bukharaev) and supported by the Kazan Federal University Strategic Academic Leadership Program (PRIORITY-2030) (S.A. Ziganshina, M.A. Ziganshin).

Figure Captions

Fig. 1. Structural formula of the dipeptide AlaPhe.

Fig. 2. AFM images of the AlaPhe films obtained from the solution in MeOH (1 mg/mL) (a) and HFIP (1 mg/mL) (b) by self-drying.

Fig. 3. AFM images of the AlaPhe films obtained from the solution in MeOH (1 mg/mL) (a) and HFIP (1 mg/mL) (b) by forced drying.

Fig. 4. AFM images of the AlaPhe films obtained from the solution in MeOH (1 mg/mL) (a) and HFIP (1 mg/mL) (b) by forced drying after saturation with MeOH vapor for 10 min.

Fig. 5. AFM images of the AlaPhe films obtained from the solution in methanol (1 mg/mL) (a) and HFIP (1 mg/mL) (b) by forced drying after saturation with methanol vapor for 30 min.

Fig. 6. AFM images of the AlaPhe films obtained from the solution in MeOH (1 mg/mL) (a) and HFIP (1 mg/mL) (b) by forced drying after saturation with MeOH vapor for 60 min.

Fig. 7. Curves obtained in the atomic force spectroscopy mode for an amorphous AlaPhe film.

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