Delving into the Latest Updates on Trypsin with Synapse

Overview

Basic Info

Drug Type

Chemical drugs

Synonyms-

Target-

Action-

Mechanism-

Therapeutic Areas

Other DiseasesRespiratory Diseases

Active Indication

HematomaPulmonary Emphysema

Inactive Indication-

Originator Organization-

Active Organization

Wuhan Healthgen Biotechnology Corp.

Inactive Organization-

License Organization

Sun Pharmaceutical Industries Ltd.

Aksigen Hospital Care

Drug Highest PhaseApproved

First Approval Date-

Regulation-

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Pain is a very important factor in Endodontic treatment, Both intra- and Post-operatively. In case of symptomatic Irreversible pulpitis, a build up of inflammatory mediators makes it very difficult for the operator to reach the desired level of anesthesia in order to deliver a pain free treatment as well as to eliminate or at least reduce post-operative pain incidence and severity. therefore, a number of pre- medications was suggested with variable success rates. Therefore this trial aims at the use of a new category of anti-inflammatory medications which would be less harmful than the standard NSAIDs or steroids.

Start Date15 Jun 2025

Sponsor / Collaborator

Cairo University

[+1]

CTRI/2025/04/085392

/ Not yet recruitingPhase 2/3IIT

Evaluation of the Effectiveness of Glucosamine and Bromelain-Trypsin-Rutoside Combination Gel in the Management of Myogenous and Disc Disorders of Temporomandibular Joint- A Randomised Clinical Trial - NIL

Start Date05 May 2025

Sponsor / Collaborator-

TCTR20250218022

/ RecruitingNot ApplicableIIT

A Preliminary Study on the Ability of a Trypsin Like Peptidase Activity Assay Kit in Detecting Periodontitis among patients visiting the College of Dental Medicine Rangsit University

Start Date16 Feb 2025

Sponsor / Collaborator

Rangsit University

100 Clinical Results associated with Trypsin

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100 Translational Medicine associated with Trypsin

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100 Patents (Medical) associated with Trypsin

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4,899

Literatures (Medical) associated with Trypsin

01 Aug 2025·Bioelectrochemistry

Exploring the electrochemical behaviour of digestive enzymes at a liquid|liquid micro-interface array

Article

Author: Arrigan, Damien W M ; Zannah, Shaheda

Trypsin and pepsin are proteolytic enzymes secreted by the digestive system to digest proteins. Here, we examine the electrochemical behaviour and detection of trypsin and pepsin at a liquid/liquid (L|L) micro-interface array. For both proteins, aqueous phase of 10 mM hydrochloric acid was the only electrolyte solution in which they were electroactive. Neither protein was detected below 30 μM by cyclic voltammetry (CV) but stripping voltammetry following adsorption (AdSV) enabled the detection of sub-micromolar concentrations of both proteins. Although pepsin was electroactive at the micro-interface array in aqueous phase of 10 mM HCl, its behaviour was ill-defined and unsuitable for characterization by CV. It was found that pepsin easily blocked the micro-interfaces, as seen by greatly hampered ion transfer voltammetry of tetrapropylammonium ion (TPrA⁺) whereas trypsin only slightly impeded TPrA⁺ transfer. This highlights the dissimilarity between pepsin and trypsin. These results illustrate the rich viability of electrochemistry at L|L micro-interface arrays as a tool to explore the behaviour and detection of biological macromolecules.

01 Jun 2025·Analytica Chimica Acta

Online multimethod platform for comprehensive characterization of monoclonal antibodies in cell culture fluid from injection of crude sample - Incorporation of middle-up and bottom-up workflows

Article

Author: Lubbers, Karin ; Haselberg, Rob ; Wouters, Sam ; Vido, Marek ; Gargano, Andrea F G ; de Kleijne, Vera H ; Zioga, Eirini ; Somsen, Govert W ; Sadighi, Raya

BACKGROUNDDetermination of critical quality attributes (CQAs) of pharmaceutical monoclonal antibodies (mAbs) is an essential part of quality control. Commonly, for each CQA, a separate analytical method and setup is required, making assessment of multiple CQAs time-consuming and labour-intensive. This typically involves offline purification and diverse protein digestion steps, in combination with multiple liquid-chromatographic modes. We developed an integrated, fully online multidimensional platform for direct analysis of mAbs in cell culture fluid (CCF) at an intact, subunit and peptide level from a single injection.RESULTSThis paper focuses on the online middle-up and bottom-up workflows. The platform combines Protein A affinity chromatography (ProtA), immobilized enzyme reactors (IMERs), reversed-phase liquid chromatography (RPLC) and high-resolution mass spectrometry (MS) for characterization of mAbs. Online ProtA was used to isolate mAbs directly from CCF. Subsequent online digestion of isolated mAb was accomplished by IMERs featuring either the proteases IdeS or trypsin. Between ProtA and IMERs, buffer exchange and pH adjustment were achieved using a strong cation-exchange (SCX) trap column. RPLC-MS analysis of F(ab)'₂ and Fc/2 fragments obtained after IdeS digestion provided information on mAb glycoform compositions and the potential presence of PTMs and subunit variants. RPLC-MS/MS analysis of trypsin-digested peptides provided over 95 % coverage of the mAb's amino acid sequence, but also identification and localization of modifications related to e.g. oxidation and deamidation. Comparisons with established offline methods were made. The overall capacity of the system to perform intact, middle-, and bottom-up analyses in parallel from a single injection is demonstrated for an industrially-relevant mAb in CCF.SIGNIFICANCEThe developed multidimensional platform enables the simultaneous characterization of multiple fractions from a single ProtA-isolated mAb band at intact, middle-up, or bottom-up level using various LC modes at a substantially reduced analysis time.

01 May 2025·International Journal of Biological Macromolecules

Enhancement on the solubility of polyploid and diploid rice proteins by enzymatic hydrolysis: From structural and functional characteristics of rice protein hydrolysates

Article

Author: Niu, Meng ; Li, Qiong ; Zhao, Siming ; Xu, Yan ; Jia, Caihua

Polyploid rice protein (PRP) has the advantage of high nutritional value, but its functional properties are minimal due to its poor solubility. This work aims to improve the solubility of PRP through enzymatic hydrolysis and assess the effect of hydrolysis time (5-330 min) and protease type (Alcalase, Neutrase, and Trypsin) on the structural, functional, and antioxidant properties of PRP hydrolysates (PRPHs). Compared to PRP, PRPHs exhibited significantly decreased free sulfhydryl content and surface hydrophobicity and improved structural flexibility, regardless of the protease used. With increasing time, the nitrogen solubility index of the hydrolysates increased by 25.01 %, which was attributed to the reduction in molecular weight (< 15 kDa). The highest emulsifying activity (48.81 m²/g) and hydroxyl radical scavenging activity (IC₅₀ of 5.49 mg/mL) were observed from Neutrase hydrolysates at 210 min and 330 min, respectively. Trypsin hydrolysate at 210 min demonstrated the lowest IC₅₀ (0.17 mg/mL) in ABTS⁺. Moreover, compared to diploid rice protein hydrolysates (DRPHs) obtained under the same conditions, PRPHs by all proteases exhibited superior functional and antioxidant properties and richer amino acid content. This study showed the potential of PRPHs applied to functional foods with favorable functional and antioxidant properties.

100 Deals associated with Trypsin

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