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Last update 08 May 2025

XPNPEP2

Last update 08 May 2025

Basic Info

Synonyms

Aminoacylproline aminopeptidase, mAmP, Membrane-bound aminopeptidase P

+ [7]

Introduction

Membrane-bound metalloprotease which catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. May play a role in the metabolism of the vasodilator bradykinin.

Drugs associated with XPNPEP2

ST-115

Target

XPNPEP2

Mechanism

XPNPEP2 inhibitors

Active Org.

Loyola University of Chicago

Originator Org.

Loyola University of Chicago

Active Indication

Ischemic stroke [+1]

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with XPNPEP2

100 Translational Medicine associated with XPNPEP2

0 Patents (Medical) associated with XPNPEP2

128

Literatures (Medical) associated with XPNPEP2

10 Apr 2025·ACS Medicinal Chemistry Letters

Development of a Cyclic TMTP1-Based PET Probe for Visualization of Hepatocellular Carcinoma

Article

Author: Wang, Min ; Meng, Zihan ; Tan, Boyu ; Zhu, Jiamin ; Qu, Chunrong ; Cheng, Zhen

TMTP1 is a tumor-homing peptide that selectively targets highly metastatic tumor cells with XPNPEP2 identified as its potential targeting receptor. Although TMTP1-based molecular probes have been explored for imaging tumors such as hepatocellular carcinoma (HCC), their clinical translation has been hampered by factors including suboptimal tumor uptake and rapid systemic clearance. To study possible solution for addressing these challenges, a cyclic TMTP1 based positron emission tomography (PET) probe, [⁶⁸Ga]Ga-DOTA-cTMTP1, was designed, synthesized, and evaluated for imaging HCC in small animal models. [⁶⁸Ga]Ga-DOTA-cTMTP1 demonstrated favorable aqueous solubility, with a log D _7.4 value of -3.28 ± 0.05, and it exhibited excellent in vitro stability in phosphate buffered saline (PBS) and fetal bovine serum (FBS). Biodistribution studies revealed a certain level of tumor accumulation (0.98 ± 0.14%ID/g at 30 min) and retention (0.40 ± 0.11%ID/g at 120 min). Impressively, [⁶⁸Ga]Ga-DOTA-cTMTP1 maintained high tumor-to-liver contrast over time, with ratios of 2.65 ± 0.45 at 30 min, 2.37 ± 0.07 at 60 min, and 2.14 ± 0.20 at 120 min. It also displayed capability of clear visualization of small HCC foci (<4 mm) in transgenic c-Myc liver tumor mice models, with tumor/liver ratios 2.20 ± 0.10 at 30 min, 2.26 ± 0.11 at 60 min, and 2.55 ± 0.44 at 120 min, respectively. Overall, this study highlights that [⁶⁸Ga]Ga-DOTA-cTMTP1 has favorable pharmacokinetic and in vivo tumor imaging profile, and it is a highly promising probe for visualization of HCC microlesions. Development of PET probes based on cyclic TMTP1 is a promising approach for discovering novel imaging probes.

01 Feb 2025·European Journal of Sport Science

Validity and Inter‐Device Reliability of an Artificial Intelligence App for Real‐Time Assessment of 505 Change of Direction Tests

Article

Author: Molina‐López, Jorge ; Jones, Paul A. ; Almagro, Bartolomé J. ; Barrera‐Domínguez, Francisco J.

ABSTRACTThe present study aimed to explore the validity and inter‐device reliability of a novel artificial intelligence app (Asstrapp) for real‐time measurement of the traditional (tra505) and modified‐505 (mod505) change of direction (COD) tests. Twenty‐five male Sports Science students (age, 23.5 ± 3.27 years; body height, 178 ± 9.76 cm; body mass, 79.4 ± 14.7 kg) completed 12 trials each, consisting of six tra505 and six mod505 trials. Completion times were simultaneously recorded via single‐beam electronic timing gates (ETG) and two different iPhones (APP1 and APP2). In total 300 trials were collected across the two tests, using all three devices, to establish the reliability and validity of the app. The coefficient of variation indicated a similar level of dispersion between the ETG (≤ 2.73%), APP1 (≤ 2.39%) and APP2 (≤ 2.52%). Intraclass correlation coefficients (ICC) revealed excellent reliability among the three timing devices (ICC ≥ 0.99) and Asstrapp relative reliability was excellent for both APP1 (ICC ≥ 0.91) and APP2 (ICC ≥ 0.91). There was a practically perfect correlation and agreement between ETG and Asstrapp (APP1: r = 0.97; APP2: r = 0.97) for both COD tests. However, small but significant differences were found between smartphones and ETG for tra505 (ES ≤ 0.33; p < 0.05). Collectively, these findings support the use of Asstrapp for real‐time assessment of both 505 COD tests.

10 Dec 2024·Proceedings of the National Academy of Sciences

Magnetochrome-catalyzed oxidation of ferrous iron by MamP enables magnetite crystal growth in the magnetotactic bacterium AMB-1

Article

Author: Faivre, Damien ; Choueikani, Fadi ; Siponen, Marina I. ; Amor, Matthieu ; Chevrier, Daniel M. ; Li, Chenghao ; Marcano, Lourdes ; Egli, Ramon ; Scoppola, Ernesto

Magnetotactic bacteria have evolved the remarkable capacity to biomineralize chains of magnetite [Fe(II)Fe(III) 2 O 4 ] nanoparticles that align along the geomagnetic field and optimize their navigation in the environment. Mechanisms enabling magnetite formation require the complex action of numerous proteins for iron acquisition, sequestration in dedicated magnetosome organelles, and precipitation into magnetite. The MamP protein contains c-type cytochromes called magnetochrome domains that are found exclusively in magnetotactic bacteria. Ablation of magnetochromes in MamP prevents bacteria from aligning with external magnetic fields, showing their importance to maintain this biological function. MamP has been proposed, mostly from in vitro experimentations, to regulate iron redox state and maintain an Fe(II)/Fe(III) balance compatible with magnetite formation via the iron oxidase activity of magnetochromes. To test the proposed function for MamP in vivo in the magnetotactic strain Magnetospirillum magneticum (AMB)-1, we characterized the iron species in chemical MamP-mediated magnetite syntheses as well as in bacteria unable to produce MamP using a combination of physicochemical methodologies. We show that MamP has no apparent control on the speciation and oxidation state of intracellular iron or on the Fe(II)/Fe(III) balance in magnetite. We propose that MamP promotes magnetite growth by incorporating Fe(III) into preexisting magnetite seeds and that magnetite structure and stoichiometry is maintained by further equilibration with dissolved Fe(II) in magnetosome organelles.

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XPNPEP2

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