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Control of Surface-Localized, Enzyme-Assisted Self-Assembly of Peptides through Catalyzed Oligomerization

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† Université de Strasbourg, CNRS, Institut Charles Sadron UPR 22, 23 rue du Loess, F-67034 Strasbourg Cedex, France
‡ Université de Strasbourg, CNRS, CMC UMR 7140, F-67000, Strasbourg, France
§ Dipartimento di Scienze, Università degli Studi della Basilicata, via dell’Ateneo Lucano, 85100 Potenza, Italy
∥ INSERM, Unité 1121 “Biomaterials and Bioengineering”, 11 rue Humann, F-67085 Strasbourg Cedex, France
⊥ Université de Strasbourg, Faculté de Chirurgie Dentaire, Fédération de Médecine Translationnelle de Strasbourg (FMTS), and Fédération des Matériaux et Nanoscience d’Alsace (FMNA), 8 rue Sainte Elisabeth, F-67000 Strasbourg, France
# University of Strasbourg Institute for Advanced Study, 5 allée du Général Rouvillois, F-67083 Strasbourg, France
*E-mail: [email protected]. Tel: +33-3-88-41-40-12 and +33-3-67-85-33-87 (P.S.).
*E-mail: [email protected]; Tel: +33-3-88-41-41-60 (F.B.).
Cite this: Langmuir 2017, 33, 33, 8267–8276
Publication Date (Web):July 27, 2017
https://doi.org/10.1021/acs.langmuir.7b01532
Copyright © 2017 American Chemical Society
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    Abstract

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    Localized self-assembly allowing both spatial and temporal control over the assembly process is essential in many biological systems. This can be achieved through localized enzyme-assisted self-assembly (LEASA), also called enzyme-instructed self-assembly, where enzymes present on a substrate catalyze a reaction that transforms noninteracting species into self-assembling ones. Very few LEASA systems have been reported so far, and the control of the self-assembly process through the surface properties represents one essential step toward their use, for example, in artificial cell mimicry. Here, we describe a new type of LEASA system based on α-chymotrypsin adsorbed on a surface, which catalyzes the production of (KL)nOEt oligopeptides from a KLOEt (K: lysine; L: leucine; OEt ethyl ester) solution. When a critical concentration of the formed oligopeptides is reached near the surface, they self-assemble into β-sheets resulting in a fibrillar network localized at the interface that can extend over several micrometers. One significant feature of this process is the existence of a lag time before the self-assembly process starts. We investigate, in particular, the effect of the α-chymotrypsin surface density and KLOEt concentration on the self-assembly kinetics. We find that the lag time can be finely tuned through the surface density in α-chymotrypsin and KLOEt concentration. For a given surface enzyme concentration, a critical KLOEt concentration exists below which no self-assembly takes place. This concentration increases when the surface density in enzyme decreases.

    Supporting Information

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    List of chemicals, detailed synthesis of KLOEt and α-chymotrypsinFITC, image of the specific homemade cryo-holder, gelation test of KLOEt and α-chymotrypsin mixture in solution, QCM-D experiments using adsorbed BSA in comparison with adsorbed α-chymotrypsin, MALDI-TOF spectra of (KL)nOEt hydrogel obtained on PEI/TA/α-chymotrypsin, second structure analysis of (KL)7OEt oligomers by MD, Cryo-SEM image of a peptide network after 40 min of self-assembly, Evolution of the optical density of pNPA in solution with KL6OEt, schematic representation of the lag time estimation, evolution of α-chymotrypsinFITC density as a function of the molar ratio in enzyme of the solution deposited, nucleophilic activity of (KL)nOEt self-assembled hydrogel measured at different times for rsurface = 100% and 5%. The Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/acs.langmuir.7b01532.

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