scholarly journals Peptidyl Activity-Based Probes for Imaging Serine Proteases

2021 ◽  
Vol 9 ◽  
Author(s):  
Paulina Kasperkiewicz
Keyword(s):  
Posttranslational Modifications ◽  
Serine Proteases ◽  
Visual Observation ◽  
Biological Processes ◽  
Basic Principles ◽  
Peptide Bonds ◽  
Endogenous Inhibitors ◽  
Hydrolysis Of ◽  
Enormous Number

Proteases catalyze the hydrolysis of peptide bonds. Products of this breakdown mediate signaling in an enormous number of biological processes. Serine proteases constitute the most numerous group of proteases, accounting for 40%, and they are prevalent in many physiological functions, both normal and disease-related functions, making them one of the most important enzymes in humans. The activity of proteases is controlled at the expression level by posttranslational modifications and/or endogenous inhibitors. The study of serine proteases requires specific reagents not only for detecting their activity but also for their imaging. Such tools include inhibitors or substrate-related chemical molecules that allow the detection of proteolysis and visual observation of active enzymes, thus facilitating the characterization of the activity of proteases in the complex proteome. Peptidyl activity-based probes (ABPs) have been extensively studied recently, and this review describes the basic principles in the design of peptide-based imaging agents for serine proteases, provides examples of activity-based probe applications and critically discusses their strengths, weaknesses, challenges and limitations.

scholarly journals Recognition of protein-linked glycans as a determinant of peptidase activity

2017 ◽  
Vol 114 (5) ◽  
pp. E679-E688 ◽  
Author(s):  
Ilit Noach ◽  
Elizabeth Ficko-Blean ◽  
Benjamin Pluvinage ◽  
Christopher Stuart ◽  
Meredith L. Jenkins ◽  
...  
Keyword(s):  
Posttranslational Modifications ◽  
Peptide Bond ◽  
Peptidase Activity ◽  
Peptide Bonds ◽  
Crystallographic Structures ◽  
Covalently Linked ◽  
Biochemical Analyses ◽  
Life On Earth ◽  
Glycoprotein Degradation ◽  
Hydrolysis Of

The vast majority of proteins are posttranslationally altered, with the addition of covalently linked sugars (glycosylation) being one of the most abundant modifications. However, despite the hydrolysis of protein peptide bonds by peptidases being a process essential to all life on Earth, the fundamental details of how peptidases accommodate posttranslational modifications, including glycosylation, has not been addressed. Through biochemical analyses and X-ray crystallographic structures we show that to hydrolyze their substrates, three structurally related metallopeptidases require the specific recognition of O-linked glycan modifications via carbohydrate-specific subsites immediately adjacent to their peptidase catalytic machinery. The three peptidases showed selectivity for different glycans, revealing protein-specific adaptations to particular glycan modifications, yet always cleaved the peptide bond immediately preceding the glycosylated residue. This insight builds upon the paradigm of how peptidases recognize substrates and provides a molecular understanding of glycoprotein degradation.

Proteases: a primer

2002 ◽  
Vol 38 ◽  
pp. 1-8 ◽  
Author(s):  
Nigel M Hooper
Keyword(s):  
Active Site ◽  
Serine Proteases ◽  
Cysteine Proteases ◽  
Aspartic Proteases ◽  
Peptide Bonds ◽  
Endogenous Inhibitors ◽  
Merops Database ◽  
Internal Peptide ◽  
Synthesis And Degradation

A protease can be defined as an enzyme that hydrolyses peptide bonds. Proteases can be divided into endopeptidases, which cleave internal peptide bonds in substrates, and exopeptidases, which cleave the terminal peptide bonds. Exopeptidases can be further subdivided into aminopeptidases and carboxypeptidases. The Schechter and Berger nomenclature provides a model for describing the interactions between the peptide substrate and the active site of a protease. Proteases can also be classified as aspartic proteases, cysteine proteases, metalloproteases, serine proteases and threonine proteases, depending on the nature of the active site. Different inhibitors can be used experimentally to distinguish between these classes of protease. The MEROPs database groups proteases into families on the basis of similarities in sequence and structure. Protease activity can be regulated in vivo by endogenous inhibitors, by the activation of zymogens and by altering the rate of their synthesis and degradation.

scholarly journals Identification of ‘erasers’ for lysine crotonylated histone marks using a chemical proteomics approach

eLife ◽  
2014 ◽  
Vol 3 ◽  
Author(s):  
Xiucong Bao ◽  
Yi Wang ◽  
Xin Li ◽  
Xiao-Meng Li ◽  
Zheng Liu ◽  
...  
Keyword(s):  
Posttranslational Modifications ◽  
Histone H3 ◽  
Gene Promoters ◽  
Biological Processes ◽  
Cellular Functions ◽  
Cellular Mechanisms ◽  
Chemical Proteomics ◽  
Wide Range ◽  
Proteomics Approach ◽  
Hydrolysis Of

Posttranslational modifications (PTMs) play a crucial role in a wide range of biological processes. Lysine crotonylation (Kcr) is a newly discovered histone PTM that is enriched at active gene promoters and potential enhancers in mammalian cell genomes. However, the cellular enzymes that regulate the addition and removal of Kcr are unknown, which has hindered further investigation of its cellular functions. Here we used a chemical proteomics approach to comprehensively profile ‘eraser’ enzymes that recognize a lysine-4 crotonylated histone H3 (H3K4Cr) mark. We found that Sirt1, Sirt2, and Sirt3 can catalyze the hydrolysis of lysine crotonylated histone peptides and proteins. More importantly, Sirt3 functions as a decrotonylase to regulate histone Kcr dynamics and gene transcription in living cells. This discovery not only opens opportunities for examining the physiological significance of histone Kcr, but also helps to unravel the unknown cellular mechanisms controlled by Sirt3, that have previously been considered solely as a deacetylase.

Kinetic Characterization of Anticarsia gemmatalis Digestive Serine- Proteases and the Inhibitory Effect of Synthetic Peptides

2018 ◽  
Vol 24 (11) ◽  
Author(s):  
Adriana M. Patarroyo-Vargas ◽  
Yaremis B. Merino-Cabrera ◽  
Jose C. Zanuncio ◽  
Francelina Rocha ◽  
Wellington G. Campos ◽  
...  
Keyword(s):  
Synthetic Peptides ◽  
Serine Proteases ◽  
Inhibitory Effect ◽  
Anticarsia Gemmatalis ◽  
Kinetic Characterization

scholarly journals Pretreatment of Switchgrass for Production of Glucose via Sulfonic Acid-Impregnated Activated Carbon

Processes ◽  
2021 ◽  
Vol 9 (3) ◽  
pp. 504
Author(s):  
Yane Ansanay ◽  
Praveen Kolar ◽  
Ratna Sharma-Shivappa ◽  
Jay Cheng ◽  
Consuelo Arellano
Keyword(s):  
Activated Carbon ◽  
Sulfonic Acid ◽  
Solid Acid ◽  
Methanesulfonic Acid ◽  
Biofuel Production ◽  
Acid Catalysts ◽  
Effects Of Temperature ◽  
Carbon Catalysts ◽  
Hydrolysis Of

In the present research, activated carbon-supported sulfonic acid catalysts were synthesized and tested as pretreatment agents for the conversion of switchgrass into glucose. The catalysts were synthesized by reacting sulfuric acid, methanesulfonic acid, and p-toluenesulfonic acid with activated carbon. The characterization of catalysts suggested an increase in surface acidities, while surface area and pore volumes decreased because of sulfonation. Batch experiments were performed in 125 mL serum bottles to investigate the effects of temperature (30, 60, and 90 °C), reaction time (90 and 120 min) on the yields of glucose. Enzymatic hydrolysis of pretreated switchgrass using Ctec2 yielded up to 57.13% glucose. Durability tests indicated that sulfonic solid-impregnated carbon catalysts were able to maintain activity even after three cycles. From the results obtained, the solid acid catalysts appear to serve as effective pretreatment agents and can potentially reduce the use of conventional liquid acids and bases in biomass-into-biofuel production.

Characterization of endogenous endopeptidases and exopeptidases and application for the limited hydrolysis of peanut proteins

2021 ◽  
Vol 345 ◽  
pp. 128764
Author(s):  
Yeming Chen ◽  
Hongsheng Zhang ◽  
Caimeng Zhang ◽  
Xiangzhen Kong ◽  
Yufei Hua
Keyword(s):  
Peanut Proteins ◽  
Hydrolysis Of

scholarly journals Multifunctional Biodegradable Vascular PLLA Scaffold with Improved X-ray Opacity, Anti-Inflammation, and Re-Endothelization

Polymers ◽  
2021 ◽  
Vol 13 (12) ◽  
pp. 1979
Author(s):  
Ho In Lee ◽  
Yun Heo ◽  
Seung-Woon Baek ◽  
Da-Seul Kim ◽  
Duck Hyun Song ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Inflammatory Responses ◽  
Neointimal Hyperplasia ◽  
Film Surface ◽  
High Mechanical Property ◽  
X Ray ◽  
Stent Restenosis ◽  
X Ray Computed ◽  
Hydrolysis Of

Poly(L-lactic acid) (PLLA) has been used as a biodegradable vascular scaffold (BVS) material due to high mechanical property, biodegradability, and biocompatibility. However, acidic byproducts from hydrolysis of PLLA reduce the pH after the surrounding implanted area and cause inflammatory responses. As a result, severe inflammation, thrombosis, and in-stent restenosis can occur after implantation by using BVS. Additionally, polymers such as PLLA could not find on X-ray computed tomography (CT) because of low radiopacity. To this end, here, we fabricated PLLA films as the surface of BVS and divided PLLA films into two coating layers. At the first layer, PLLA film was coated by 2,3,5-triiodobenzoic acid (TIBA) and magnesium hydroxide (MH) with poly(D,L-lactic acid) (PDLLA) for radiopaque and neutralization of acidic environment, respectively. The second layer of coated PLLA films is composed of polydopamine (PDA) and then cystamine (Cys) for the generation of nitric oxide (NO) release, which is needed for suppression of smooth muscle cells (SMCs) and proliferation of endothelial cells (ECs). The characterization of the film surface was conducted via various analyses. Through the surface modification of PLLA films, they have multifunctional abilities to overcome problems of BVS effectively such as X-ray penetrability, inflammation, thrombosis, and neointimal hyperplasia. These results suggest that the modification of biodegradable PLLA using TIBA, MH, PDA, and Cys will have important potential in implant applications.

scholarly journals TESTS FOR HYDROLYSIS OF PEPTIDE BONDS BY ULTRAVIOLET LIGHT

1950 ◽  
Vol 187 (2) ◽  
pp. 543-545
Author(s):  
Dorothy J. McLean ◽  
Arthur C. Giese
Keyword(s):  
Ultraviolet Light ◽  
Peptide Bonds ◽  
Hydrolysis Of
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