Identification of a methotrexate-binding peptide from a T7 phage display screen using a QCM device.
An 11-mer unique peptide sequence SIFPLCNSGAL was identified as a methotrexate (MTX)-binding peptide from a T7 phage display screen using a quartz-crystal microbalance (QCM) biosensor. The synthetic peptide displayed weak interaction with MTX (K(D) 2.23x10(-5) M) using surface plasmon resonance (SPR). Interestingly, analysis of the primary amino acid sequence of the peptide identified similarities to the MTX-binding site of dihydrofolate reductase (DHFR). Our results highlight the importance of this primary sequence for the recognition of the MTX molecule.
Takakusagi
Yoichi
Y
Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan.
Kuroiwa
Yuki
Y
Sugawara
Fumio
F
Sakaguchi
Kengo
K
D000595:Amino Acid Sequence; D015374:Biosensing Techniques / Q000295:instrumentation*; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D058973:Folate Receptors, GPI-Anchored; D008727:Methotrexate / Q000737:chemistry / Q000494:pharmacology; D008958:Models, Molecular; D015394:Molecular Structure; D019151:Peptide Library; D011956:Receptors, Cell Surface / Q000737:chemistry* / Q000378:metabolism; D013762:Tetrahydrofolate Dehydrogenase / Q000378:metabolism
D002352:Carrier Proteins; D058973:Folate Receptors, GPI-Anchored; D019151:Peptide Library; D011956:Receptors, Cell Surface; D013762:Tetrahydrofolate Dehydrogenase; D008727:Methotrexate