دورية أكاديمية
أعرض في EDS

Enhanced Tumor Targeting and Antitumor Activity of Methylated β-Cyclodextrin-Threaded Polyrotaxanes by Conjugating Cyclic RGD Peptides.

التفاصيل البيبلوغرافية
العنوان: Enhanced Tumor Targeting and Antitumor Activity of Methylated β-Cyclodextrin-Threaded Polyrotaxanes by Conjugating Cyclic RGD Peptides.
المؤلفون: Zhang S; Department of Organic Biomaterials, Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University (TMDU), 2-3-10 Kanda-Surugadai, Chiyoda, Tokyo 101-0062, Japan., Tamura A; Department of Organic Biomaterials, Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University (TMDU), 2-3-10 Kanda-Surugadai, Chiyoda, Tokyo 101-0062, Japan., Yui N; Department of Organic Biomaterials, Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University (TMDU), 2-3-10 Kanda-Surugadai, Chiyoda, Tokyo 101-0062, Japan.
المصدر: Biomolecules [Biomolecules] 2024 Feb 15; Vol. 14 (2). Date of Electronic Publication: 2024 Feb 15.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: MDPI Country of Publication: Switzerland NLM ID: 101596414 Publication Model: Electronic Cited Medium: Internet ISSN: 2218-273X (Electronic) Linking ISSN: 2218273X NLM ISO Abbreviation: Biomolecules Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Basel, Switzerland : MDPI, 2011-
مواضيع طبية MeSH: Rotaxanes*/pharmacology , Rotaxanes*/chemistry , Rotaxanes*/metabolism , beta-Cyclodextrins*/chemistry , Neoplasms*/drug therapy , Peptides, Cyclic*, Humans ; Oligopeptides/chemistry ; Integrins
مستخلص: We previously reported that acid-degradable methylated β-cyclodextrins (Me-β-CDs)-threaded polyrotaxanes (Me-PRXs) can induce autophagic cell death through endoplasmic reticulum (ER) stress-related autophagy, even in apoptosis-resistant cells. Hence, Me-PRXs show great potential as anticancer therapeutics. In this study, peptide-supermolecule conjugates were designed to achieve the targeted delivery of Me-PRX to malignant tumors. Arg-Gly-Asp peptides are well-known binding motifs of integrin α v β 3 , which is overexpressed on angiogenic sites and many malignant tumors. The tumor-targeted cyclic Arg-Gly-Asp (cRGD) peptide was orthogonally post-modified to Me-PRX via click chemistry. Surface plasmon resonance (SPR) results indicated that cRGD-Me-PRX strongly binds to integrin α v β 3 , whereas non-targeted cyclic Arg-Ala-Glu (cRGE) peptide conjugated to Me-PRX (cRGE-Me-PRX) failed to interact with integrins α v β 3 . In vitro, cRGD-Me-PRX demonstrated enhanced cellular internalization and antitumor activity in 4T1 cells than that of unmodified Me-PRX and non-targeted cRGE-Me-PRX, due to its ability to recognize integrin α v β 3 . Furthermore, cRGD-Me-PRX accumulated effectively in tumors, leading to antitumor effects, and exhibited excellent biocompatibility and safety in vivo. Therefore, cRGD conjugation to enhance selectivity for integrin α v β 3 -positive cancer cells is a promising design strategy for Me-PRXs in antitumor therapy.
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معلومات مُعتمدة: JP20H04527 Japan Society for the Promotion of Science
فهرسة مساهمة: Keywords: antitumor activity; cyclic RGD peptide; methylated β-cyclodextrin; polyrotaxane; tumor targeting
المشرفين على المادة: 78VO7F77PN (arginyl-glycyl-aspartic acid)
0 (cyclic arginine-glycine-aspartic acid peptide)
0 (Rotaxanes)
0 (beta-Cyclodextrins)
0 (Oligopeptides)
0 (Integrins)
0 (Peptides, Cyclic)
تواريخ الأحداث: Date Created: 20240224 Date Completed: 20240226 Latest Revision: 20240227
رمز التحديث: 20240227
مُعرف محوري في PubMed: PMC10886891
DOI: 10.3390/biom14020223
PMID: 38397461
قاعدة البيانات: MEDLINE
الوصف
تدمد:2218-273X
DOI:10.3390/biom14020223