Articles by Pau Gorostiza in JoVE
로컬 컨트롤 표면 점착을 고르지 Nanopatterns Dendrimer 기반: Chondrogenic 차별화 하는 방법 Ignasi Casanellas1,2, Anna Lagunas3,1, Iro Tsintzou1, Yolanda Vida4,5, Daniel Collado4,5, Ezequiel Pérez-Inestrosa4,5, Cristina Rodríguez-Pereira6, Joana Magalhaes3,6, Pau Gorostiza1,3,7, José A. Andrades8,3, José Becerra8,3,5, Josep Samitier1,3,2 1Institute for Bioengineering of Catalonia (IBEC), The Barcelona Institute of Science and Technology (BIST), 2Department of Engineering Electronics, University of Barcelona (UB), 3Networking Biomedical Research Center (CIBER), 4Instituto de Investigacin Biomédica de Málaga (IBIMA), Department of Organic Chemistry, Universidad de Málaga (UMA), 5Andalusian Centre for Nanomedicine and Biotechnology-BIONAND, 6Unidad de Bioingeniería Tisular y Terapia Celular (GBTTC-CHUAC), Grupo de Reumatolog ía, Instituto de Investigación Biomèdica de A Coruña (INIBIC), Complexo Hospitalario Universitario de A Coruña (CHUAC), Sergas, Universidade da Coruña (UDC), 7Institució Catalana de Recerca i Estudis Avançats (ICREA), 8Instituto de Investigación Biomédica de Málaga (IBIMA), Department of Cell Biology, Genetics and Physiology, Universidad de Málaga (UMA) 받는 dendrimer 기반 고르지 nanopatterns 로컬 아르기닌-글리신-aspartic 산 (RGD) 표면 밀도의 나노 제어를 허용 하는 방법은 설명 하 고 세포 접착 및 chondrogenic 분화의 연구에 대 한 적용.
Other articles by Pau Gorostiza on PubMed
Absence of a Stable Secondary Structure is Not a Limitation for Photoswitchable Inhibitors of β-arrestin/β-Adaptin 2 Protein-protein Interaction Chemistry & Biology. Jan, 2015 | Pubmed ID: 25615951 Many protein-protein interactions (PPIs) are mediated by short, often helical, linear peptides. Molecules mimicking these peptides have been used to inhibit their PPIs. Recently, photoswitchable peptides with little secondary structure have been developed as modulators of clathrin-mediated endocytosis. Here we perform a systematic analysis of a series of azobenzene-crosslinked peptides based on a β-arrestin P-long 20-mer peptide (BAP-long) sequence to assess the relevance of secondary structure in their interaction with β-adaptin 2 and to identify the design requirements for photoswitchable inhibitors of PPI (PIPPIs). We observe that flexible structures show a greater inhibitory capacity and enhanced photoswitching ability and that the absence of helical structures in free inhibitor peptide is not a limitation for PIPPI candidates. Therefore, our PIPPIs expand the field of potential inhibitors of PPIs to the wide group of flexible peptides, and we argue against using a stable secondary structure as a sole criterion when designing PIPPI candidates.
OptoGluNAM4.1, a Photoswitchable Allosteric Antagonist for Real-Time Control of MGlu4 Receptor Activity Cell Chemical Biology. Aug, 2016 | Pubmed ID: 27478159 OptoGluNAM4.1, a negative allosteric modulator (NAM) of metabotropic glutamate receptor 4 (mGlu4) contains a reactive group that covalently binds to the receptor and a blue-light-activated, fast-relaxing azobenzene group that allows reversible receptor activity photocontrol in vitro and in vivo. OptoGluNAM4.1 induces light-dependent behavior in zebrafish and reverses the activity of the mGlu4 agonist LSP4-2022 in a mice model of chronic pain, defining a photopharmacological tool to better elucidate the physiological roles of the mGlu4 receptor in the nervous system.