In Vitro Characterization and in Vivo Application of a Dual Functional Peptide

Chen, Chien-Jung; Kuo, Ping-Hsueh; Hung, Ta-Jen; Fang, Shun-lung; Yang, Chung-Hsin; Yang, Shieh‐Yueh; Chang, Margaret Dah‐Tsyr

doi:10.1109/cisis.2013.104

Cited by 1 publication

(2 citation statements)

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“…Even though specific protein receptors for CPP ecp and crotamine remain to be investigated, HSPG acting as coreceptor is indispensable for the translocation of CPP ecp and crotamine [ 12 , 34 ]. In addition, both CPP ecp and crotamine targeted highly proliferating cells such as tumor tissues [ 14 , 57 ]. Interestingly, a motif decorating a hydrophilic aromatic amino acid participating in membrane permeation between two arginines (RWR) appeared to be conserved in both CPP ecp and crotamine, leading to similar characteristics of these 2 multifunctional HS-binding CPPs.…”

Section: Resultsmentioning

confidence: 99%

“…Cell surface negatively charged HS initializes the contact of CPPs, so particular HS binding CPPs might own mysterious sequence to exert multiple functions including HS binding, cellular binding, lipid binding, and in vivo tissue targeting activities. CPP ecp is a recently identified CPP not only binding to negatively charged molecules including GAGs and lipids on cell surface in vitro but also targeting mucosal tissues in vivo [ 12 – 14 ]. In this study, we aim to collect and analyze the characteristics of HS-binding cell penetrating peptides derived from natural proteins.…”

Section: Introductionmentioning

confidence: 99%

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A Heparan Sulfate-Binding Cell Penetrating Peptide for Tumor Targeting and Migration Inhibition

Chen

Tsai

Kuo

et al. 2015

BioMed Research International

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As heparan sulfate proteoglycans (HSPGs) are known as co-receptors to interact with numerous growth factors and then modulate downstream biological activities, overexpression of HS/HSPG on cell surface acts as an increasingly reliable prognostic factor in tumor progression. Cell penetrating peptides (CPPs) are short-chain peptides developed as functionalized vectors for delivery approaches of impermeable agents. On cell surface negatively charged HS provides the initial attachment of basic CPPs by electrostatic interaction, leading to multiple cellular effects. Here a functional peptide (CPPecp) has been identified from critical HS binding region in hRNase3, a unique RNase family member with in vitro antitumor activity. In this study we analyze a set of HS-binding CPPs derived from natural proteins including CPPecp. In addition to cellular binding and internalization, CPPecp demonstrated multiple functions including strong binding activity to tumor cell surface with higher HS expression, significant inhibitory effects on cancer cell migration, and suppression of angiogenesis in vitro and in vivo. Moreover, different from conventional highly basic CPPs, CPPecp facilitated magnetic nanoparticle to selectively target tumor site in vivo. Therefore, CPPecp could engage its capacity to be developed as biomaterials for diagnostic imaging agent, therapeutic supplement, or functionalized vector for drug delivery.

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