Related Experiment Video
Updated: May 23, 2025

Thermostabilization, Expression, Purification, and Crystallization of the Human Serotonin Transporter Bound to S-citalopram
Published on: November 27, 2016
Effect of Spacers on the Affinity of Tyrosine-Modified Polymers to L-Type Amino Acid Transporter 1
Yan Ming Voon1,2, Haochen Guo1,2,3, Kaito Kanamori1,2
1Laboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, 4259 Nagatsutacho, Midori-ku, Yokohama, Kanagawa 226-8503, Japan.
Abstract:
L-type amino acid transporter 1 (LAT1), which takes up neutral amino acids such as tyrosine, is overexpressed on various cancer cells, and many researchers have developed LAT1-targeting drug delivery systems (DDSs) by modifying them with substrates of LAT1. However, none of the previous studies have examined the effects of spacers conjugated with substrates on the interaction between the DDSs and LAT1. Here, we developed polymers with tyrosine-based ligands on the side chains via propyl- or triethylene glycol spacers and compared their targetability to that of LAT1. While both polymers exhibited efficient cellular uptake in cancer cells through endocytosis in an LAT1-selective manner, the polymer with the triethylene glycol spacers exhibited higher cellular uptake efficiency than that with the propyl-spacers. Consistently, in the in vivo study with mice bearing subcutaneous tumors, the polymer with the triethylene glycol spacers showed significantly high tumor accumulation and thereby accomplished tumor-selective delivery of photosensitizers, permitting efficient antitumor activity upon photoirradiation. Our results indicate the importance of the spacer structure in designing DDSs targeting amino acid transporters.
Related Concept Videos
Carrier-Mediated Transport
Active transport involves two types of membrane-spanning transporters: uptake and efflux. Uptake transporters are expressed in the small...
Ligand Binding and Linkage
Nonlinear Pharmacokinetics: Role of Transporters
Polymorphisms occurring in drug transporters can alter...
Adrenergic Agonists: Chemistry and Structure-Activity Relationship
Aromatic ring substitutions: Substituting the aromatic ring with –OH groups at positions 3 and 4 yields catecholamines (e.g., epinephrine), which have a high affinity for adrenoceptors. Hydrogen bonding between –OH groups and receptors enhances adrenergic activity.
Separation of...
Factors Affecting Protein-Drug Binding: Drug-Related Factors
One crucial factor in drug-protein binding is the drug's lipophilicity or its affinity for fat. More lipophilic drugs tend to have higher binding extents. For example, highly lipophilic drugs like cloxacillin exhibit substantial protein binding, with as much as 95% of the drug binding to proteins. In...
Translocation of Proteins into the Mitochondria
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...

