Kanagavel Deepankumar

Vellore Institute of Technology University

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Hyungdon Yun

Konkuk University

Saravanan Prabhu Nadarajan

Tamil Nadu Agricultural University

Niraikulam Ayyadurai

Council of Scientific and Industrial Research

Ali Miserez

Nanyang Technological University

Sun‐Gu Lee

Pusan National University

Sam Mathew

University of Edinburgh

Byung‐Gee Kim

Seoul National University

Harini Mohanram

Nanyang Technological University

SunGu Lee

Heon‐Ho Jeong

Chonnam National University

Cooperative Institutions

Nanyang Technological University

Yeungnam University

Seoul National University

National University of Singapore

Government of the Republic of Korea

Centre National de la Recherche Scientifique

Konkuk University

Zhejiang University

Central Leather Research Institute

Agency for Science, Technology and Research

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Development of a Selective, Sensitive, and Reversible Biosensor by the Genetic Incorporation of a Metal‐Binding Site into Green Fluorescent Protein

Angewandte Chemie (2011)

Niraikulam Ayyadurai Saravanan Prabhu Nadarajan Kanagavel Deepankumar Sun‐Gu Lee Heon‐Ho Jeong

Wenn das Licht ausgeht: Ein Kupfer- Biosensor wurde durch gentechnischen Ersatz von L-Tyrosin in grün fluoreszierendem Protein durch die chelatisierende nichtkanonische Aminosäure L-DOPA hergestellt (siehe Bild). Die spezifische Bindung von Cu2+ durch das modifizierte Protein war reversibel und führte zu einer mit dem Cu2+-Gehalt skalierenden Fluoreszenzlöschung. EDTA=Ethylendiamintetraessigsäure. Detailed facts of importance to specialist readers are published as "Supporting Information". Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.

Fluorescent protein

10.1002/ange.201008289

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Citations (16)

Liquid–Liquid Phase Separation of the Green Mussel Adhesive Protein Pvfp‐5 is Regulated by the Post‐Translated Dopa Amino Acid

Advanced Materials (2021)

Kanagavel Deepankumar Qi Guo Harini Mohanram Jessica Lim Yuguang Mu

The underwater adhesive prowess of aquatic mussels has been largely attributed to the abundant post-translationally modified amino acid l-3,4-dihydroxyphenylalanine (Dopa) in mussel foot proteins (MFPs) that make up their adhesive threads. More recently, it has been suggested that during thread fabrication, MFPs form intermediate fluidic phases such as liquid crystals or coacervates regulated by a liquid-liquid phase separation (LLPS) process. Here, it is shown that Dopa plays another central role during mussel fiber formation, by enabling LLPS of Pvfp-5β, a main MFP of the green mussel Perna viridis. Using residue-specific substitution of Tyrosine (Tyr) for Dopa during recombinant expression, Dopa-substituted Pvfp-5β is shown to exhibit LLPS under seawater-like conditions, whereas the Tyr-only version forms insoluble aggregates. Combining quantum chemistry calculations and solution NMR, a transient H-bonding network requiring the two hydroxyl groups of Dopa is found to be critical to enable LLPS in Dopa-mutated Pvfp-5β. Overall, the study suggests that Dopa plays an important role in regulating LLPS of MFPs, which may be critical to concentrate the adhesive proteins at the plaque/substrate interface and therefore produce a more robust adhesive. The findings also provide molecular-level lessons to guide biomanufacturing of protein-based materials such as bioadhesives and load-bearing fibers.

Coacervate

Residue (chemistry)

10.1002/adma.202103828

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Citations (56)

Evaluation and biosynthetic incorporation of chlorotyrosine into recombinant proteins

Biotechnology and Bioprocess Engineering (2012)

Niraikulam Ayyadurai Kanagavel Deepankumar Saravanan Prabhu Nadarajan Nediljko Budiša Hyungdon Yun

10.1007/s12257-012-0066-6

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Citations (13)

Enhancing Thermostability and Organic Solvent Tolerance of ω‐Transaminase through Global Incorporation of Fluorotyrosine

Advanced Synthesis & Catalysis (2014)

Kanagavel Deepankumar Minsu Shon Saravanan Prabhu Nadarajan Giyoung Shin Sam Mathew

Abstract Here, we have utilized the incorporation of non‐canonical amino acids as a tool kit to improve enzyme properties for organic synthesis applications. The global incorporation of 3‐fluorotyrosine (FY) into ω‐transaminase (ω‐TA) to give ω‐TA[FY] enhanced the thermostability and organic solvent tolerance without altering substrate specificity and enantioselectivity. Moreover, ω‐TA[FY] was able to completely convert 25 mM of acetophenone into ( S )‐1‐phenylethylamine ( ee >99%) in the presence of 20% DMSO (v/v) which is ∼2‐fold higher when compared to wild‐type ω‐TA. magnified image

Thermostability

Transaminase

Acetophenone

10.1002/adsc.201300706

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Citations (49)

Evaluating the role of puckering and fluorine atom in stability and folding of fluoroproline containing proteins

Biotechnology and Bioprocess Engineering (2017)

Saravanan Prabhu Nadarajan Kanagavel Deepankumar Joo‐Hyun Seo Hyungdon Yun

Fluorine

Hydroxyproline

Residue (chemistry)

Folding (DSP implementation)

Protein Stability

Thermal Stability

Protein Engineering

10.1007/s12257-017-0257-2

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Citations (10)

Protein engineering for covalent immobilization and enhanced stability through incorporation of multiple noncanonical amino acids

Biotechnology and Bioprocess Engineering (2017)

Kanagavel Deepankumar Saravanan Prabhu Nadarajan June‐Hyung Kim Hyungdon Yun

Residue (chemistry)

Thermal Stability

Protein Engineering

10.1007/s12257-017-0127-y

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Citations (14)

Supramolecular β‐Sheet Suckerin–Based Underwater Adhesives

Advanced Functional Materials (2020)

Kanagavel Deepankumar Chanoong Lim Ingmar Polte Bruno Zappone Cristina Labate

Abstract Nature has evolved several molecular strategies to ensure adhesion in aqueous environments, where artificial adhesives typically fail. One recently‐unveiled molecular design for wet‐resistant adhesion is the cohesive cross‐β structure characteristic of amyloids, complementing the well‐established surface‐binding strategy of mussel adhesive proteins based on 3,4‐ l ‐dihydroxyphenylalanine (Dopa). Structural proteins that self‐assemble into cross β‐sheet networks are the suckerins discovered in the sucker ring teeth of squids. Here, light is shed on the wet adhesion of cross‐β motifs by producing recombinant suckerin‐12, naturally lacking Dopa, and investigating its wet adhesion properties. Surprisingly, the adhesion forces measured on mica reach 70 mN m −1 , exceeding those measured for all mussel adhesive proteins to date. The pressure‐sensitive adhesion of artificial suckerins is largely governed by their cross‐β motif, as evidenced using control experiments with disrupted cross‐β domains that result in complete loss of adhesion. Dopa is also incorporated in suckerin‐12 using a residue‐specific incorporation strategy that replaces tyrosine with Dopa during expression in Escherichia coli . Although the replacement does not increase the long‐term adhesion, it contributes to the initial rapid contact and enhances the adsorption onto model oxide substrates. The findings suggest that suckerins with supramolecular cross‐β motifs are promising biopolymers for wet‐resistant adhesion.

10.1002/adfm.201907534

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Citations (47)

Multiple non-canonical amino acid incorporation for the site-specific and synergistic modification in a single protein

한국생물공학회 학술대회 (2012)

Kanagavel Deepankumar Hyungdon Yun

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Tuning of monomeric red fluorescent protein folding and stability with incorporated non-natural amino acid analogues

한국생물공학회 학술대회 (2011)

Kanagavel Deepankumar Hyungdon Yun