Selective Recognition of Amino Acids and Peptides by Small Supramolecular Receptors

To this day, the recognition and high affinity binding of biomolecules in water by synthetic receptors remains challenging, while the necessity for systems for their sensing, transport and modulation persists. This problematic is prevalent for the recognition of peptides, which not only have key roles in many biochemical pathways, as well as having pharmacological and biotechnological applications, but also frequently serve as models for the study of proteins. Taking inspiration in nature and on the interactions that occur between several receptors and peptide sequences, many researchers have developed and applied a variety of different synthetic receptors, as is the case of macrocyclic compounds, molecular imprinted polymers, organometallic cages, among others, to bind amino acids, small peptides and proteins. In this critical review, we present and discuss selected examples of synthetic receptors for amino acids and peptides, with a greater focus on supramolecular receptors, which show great promise for the selective recognition of these biomolecules in physiological conditions. We decided to focus preferentially on small synthetic receptors (leaving out of this review high molecular weight polymeric systems) for which more detailed and accurate molecular level information regarding the main structural and thermodynamic features of the receptor biomolecule assemblies is available.

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The conjugation of nonsteroidal anti-inflammatory drugs (NSAID) to small peptides for generating multifunctional supramolecular nanofibers/hydrogels

Beilstein Journal of Organic Chemistry ◽

10.3762/bjoc.9.104 ◽

2013 ◽

Vol 9 ◽

pp. 908-917 ◽

Cited By ~ 51

Author(s):

Jiayang Li ◽

Yi Kuang ◽

Junfeng Shi ◽

Yuan Gao ◽

Jie Zhou ◽

...

Keyword(s):

Amino Acids ◽

Critical Concentration ◽

Therapeutic Agents ◽

Multiple Roles ◽

Small Peptides ◽

Covalent Linkage ◽

Physiological Conditions ◽

Racemic Ibuprofen ◽

Inflammatory Drugs ◽

Anti Inflammatory

Here we report supramolecular hydrogelators made of nonsteroidal anti-inflammatory drugs (NSAID) and small peptides. The covalent linkage of Phe–Phe and NSAIDs results in conjugates that self-assemble in water to form molecular nanofibers as the matrices of hydrogels. When the NSAID is naproxen (1), the resultant hydrogelator 1a forms a hydrogel at a critical concentration (cgc) of 0.2 wt % at pH 7.0. Hydrogelator 1a, also acting as a general motif, enables enzymatic hydrogelation in which the precursor turns into a hydrogelator upon hydrolysis catalyzed by a phosphatase at physiological conditions. The conjugates of Phe–Phe with other NSAIDs, such as (R)-flurbiprofen (2), racemic flurbiprofen (3), and racemic ibuprofen (4), are able to form molecular hydrogels, except in the case of aspirin (5). After the conjugation with the small peptides, NSAIDs exhibit improved selectivity to their targets. In addition, the peptides made of D-amino acids help preserve the activities of NSAIDs. Besides demonstrating that common NSAIDs are excellent candidates to promote aromatic–aromatic interaction in water to form hydrogels, this work contributes to the development of functional molecules that have dual or multiple roles and ultimately may lead to new molecular hydrogels of therapeutic agents for topical use.

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The Discovery of Synthetic Proteolytic Peptide

10.20944/preprints201801.0106.v2 ◽

2018 ◽

Author(s):

Rina Nakamura ◽

Motomi Konishi ◽

Masanari Taniguchi ◽

Yusuke Hatakawa ◽

Toshifumi Akizawa

Keyword(s):

Amino Acids ◽

Serine Protease ◽

Proteolytic Activity ◽

Synthetic Peptide ◽

Synthetic Peptides ◽

Serine Protease Inhibitor ◽

Small Peptides ◽

Physiological Conditions ◽

Proteolytic Activities ◽

Catalytic Peptides

After screening nearly 1000 synthetic peptides, a synthetic peptide termed JAL-AK22 (KYEGHWYPEKPYKGSGFRCIHI) derived from the BoxA domain in Tob1 protein was found to activate both unfolded and folded proMMP-7. In addition, JAL-AK22 showed auto-proteolytic activity. Interestingly, the smaller derivative of JAL-AK22 termed JAL-TA9 (YKGSGFRMI) also possessed auto-proteolytic activity and cleaved 2 fragment peptides (MMP18-33 and MMP18-40) derived from the prodomain of proMMP-7 under physiological conditions. These proteolytic activities were inhibited by AEBSF, a serine protease inhibitor. Our results demonstrate that a small synthetic peptide consisting of only 9 amino acids has serine protease-like activity and activates proMMP-7 by cleaving the prodomain region. We thus propose calling small peptides possessing with protease-like activity Catalytides (catalytic peptides). We expect that our findings will stimulate the development of novel Catalytides and related applications.

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The Discovery of Synthetic Proteolytic Peptide

10.20944/preprints201801.0106.v1 ◽

2018 ◽

Author(s):

Rina Nakamura ◽

Aya Kojima ◽

Motomi Konishi ◽

Masanari Taniguchi ◽

Yusuke Hatakawa ◽

...

Keyword(s):

Amino Acids ◽

Serine Protease ◽

Proteolytic Activity ◽

Synthetic Peptide ◽

Synthetic Peptides ◽

Serine Protease Inhibitor ◽

Small Peptides ◽

Physiological Conditions ◽

Proteolytic Activities ◽

Catalytic Peptides

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A single probe to sense Al(iii) colorimetrically and Cd(ii) by turn-on fluorescence in physiological conditions and live cells, corroborated by X-ray crystallographic and theoretical studies

Dalton Transactions ◽

10.1039/c4dt01433b ◽

2015 ◽

Vol 44 (9) ◽

pp. 4123-4132 ◽

Cited By ~ 35

Author(s):

Chirantan Kar ◽

Soham Samanta ◽

Sudeep Goswami ◽

Aiyagari Ramesh ◽

Gopal Das

Keyword(s):

Live Cell Imaging ◽

Cell Imaging ◽

Selective Recognition ◽

Live Cells ◽

Paper Strip ◽

Theoretical Studies ◽

X Ray ◽

Physiological Conditions ◽

Turn On ◽

Single Probe

Selective recognition of Al3+and Cd2+by UV-Vis and fluorescence based techniques using a cinnamaldehyde functionalized conjugated ligand, and its applications in paper strip and live cell imaging.

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Luteolin Imprinted Polymer with Selective Recognition and Adsorption Performance

Materials Science Forum ◽

10.4028/www.scientific.net/msf.809-810.297 ◽

2014 ◽

Vol 809-810 ◽

pp. 297-301

Author(s):

Ping Rui Meng ◽

Liang Bo Li

Keyword(s):

Adsorption Process ◽

Selective Adsorption ◽

Methanol Solution ◽

Selective Recognition ◽

Imprinted Polymer ◽

Molecular Imprinted Polymers ◽

Adsorption Dynamics ◽

Adsorption Performance ◽

Recognition Specificity ◽

Adsorption Amount

In order to selectively separate luteolin from its crude solution, we synthesized luteolin molecular imprinted polymers (LMIP) with high recognition specificity for luteolin, using an imprinting technique. Luteolin was used as template, methanol as solvent, and N,N’-methylenebisacrylamide (MBAA) as the cross-linking. Then prepared LMIP were characterized and evaluated by scanning electron microscope (SEM) and equilibrium absorption experiments. The results showed that the cavities matching with the template molecules in size and structure were present in the LMIP. Adsorption dynamics analysis suggested that, when the adsorption time reached 4 h, the adsorption process had reached balance and the adsorption capacity was at steady state. The selective adsorption amount reached at 35.65 umol/g for the LMIP, while a lower value of 11.68 umol/g for the blank polymer (i.e. nontemplated). Relative to the corresponding blank polymer, LMIP had an excellent recognition to luteolin in methanol solution. Keywords: Molecular imprinting, Molecular recognition, Adsorbent, Luteolin

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Activation of carboxylic acids by pyrocarbonates. Synthesis of arylamides of N -protected amino acids and small peptides using dialkyl pyrocarbonates as condensing reagents

International journal of peptide & protein research ◽

10.1111/j.1399-3011.1994.tb00402.x ◽

2009 ◽

Vol 44 (1) ◽

pp. 36-48 ◽

Cited By ~ 19

Author(s):

V.F. POZDNEV

Keyword(s):

Amino Acids ◽

Carboxylic Acids ◽

Small Peptides

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On the immunological properties of penicillins

Proceedings of the Royal Society of London Series B Biological Sciences ◽

10.1098/rspb.1971.0106 ◽

1971 ◽

Vol 179 (1057) ◽

pp. 411-432 ◽

Cited By ~ 17

Keyword(s):

Proteolytic Enzyme ◽

Continuous Process ◽

Polymeric Materials ◽

Small Peptides ◽

Physiological Conditions ◽

Polymer Conjugates ◽

Protein Polymer ◽

Penicillanic Acid ◽

Insoluble Form ◽

Polyvalent Antigens

Penicilloylated proteins which may be found as impurities in 6-amino-penicillanic acid can be exhaustively digested by pronase to yield amino acids and small peptides. This degradation converts the potent polyvalent antigens into a mixture of mostly monovalent haptens which are much less immunogenic and less capable of eliciting immune reactions in sensitized animals. In order to avoid the contamination of 6-aminopenicillanic acid with a proteolytic enzyme, pronase was converted into a water insoluble form by coupling it with bromoacetyl cellulose. This insoluble derivative of pronase retains its activity and broad specificity. It can be readily removed from the medium upon completion of the impurity degradation, to be used repeatedly in a continuous process. The immunological manifestations associated with penicillins are not completely abolished by removal or degradation of protein impurities. Another important cause for these manifestations appears to be polymeric materials which are formed in penicillins. Such polymeric materials were isolated from ampicillin and shown to be capable of binding spontaneously to proteins (e.g. bovine serum albumin). The protein-polymer conjugates, which are formed under physiological conditions (pH 7.4, 37 °C), were found to be immunogenic and to provoke the formation of polymer-specific antibodies.

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