Enthalpy-driven interactions with sulfated glycosaminoglycans promote cell membrane penetration of arginine peptides

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Enthalpy-driven interactions with sulfated glycosaminoglycans promote cell membrane penetration of arginine peptides

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作者：Yuki Takechi-Haraya^a ; ^b ; ^c ; Ryo Nadai^a ; ^d ; Hitoshi Kimura^a ; ^d ; Kazuchika Nishitsuji^e ; Kenji Uchimura^f ; Kumiko Sakai-Kato^c ; Kohsaku Kawakami^g ; Akira Shigenaga^a ; Toru Kawakami^h ; Akira Otaka^a ; Hironobu Hojo^h ; Naomi Sakashita^e ; Hiroyuki Saito^a ; ^d ; ^{hsaito@mb.kyoto-phu.ac.jp" class="auth_mail" title="E-mail the corresponding author}
关键词：BLI ; biolayer interferometry ; CD ; circular dichroism ; CHO ; Chinese hamster ovary ; CLSM ; confocal laser scanning microscopy ; CS ; chondroitin sulfate ; DAPI ; 4&prime ; 6-diamidino-2-phynylindole ; DMEM/F12 ; Dulbecco's modified Eagle's medium/nutrient F-12 Ham ; FAM ; 5(6)-carboxyfluorescein ; FBS ; fetal bovine serum ; GAG ; glycosaminoglycan ; GUV ; giant unilamellar vesicle ; HS ; heparan sulfate ; ITC ; isothermal titration calorimetry ; LUV ; large unilamellar vesicle ; NMR ; nuclear magnetic resonance ; PBS ; pho
刊名：Biochimica et Biophysica Acta (BBA)-Biomembranes
出版年：2016
出版时间：June 2016
年：2016
卷：1858
期：6
页码：1339-1349
全文大小：1911 K

文摘

•: Arginine peptides bind to heparin with high affinity and favorable enthalpy gain.
•: Lysine peptides bind to heparin with low affinity and negligible binding enthalpy.
•: Binding enthalpy to heparin is correlated with cell penetration of arginine peptides.
•: A critical role of enthalpy-driven interactions of CPP with GAG is proposed.

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