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<p>Two amphiphilic peptides, Pep1 (bis(FHLAL)‑K‑RGD) and Pep2 (bis(FLIVI)‑K‑RGD), were rationally designed to achieve direct, non-covalent anchoring onto liposomal membranes for integrin-targeted drug delivery applications. The peptides were synthesized using Fmoc-based solid-phase methods and validated through high-performance liquid chromatography and mass spectrometry, confirming high purity (&gt; 95%) and expected molecular masses. In silico analysis using coarse-grained Martini molecular dynamics simulations demonstrated successful surface anchoring of both peptides to dipalmitoyl phosphatidylcholine–cholesterol bilayers, with hydrophilic RGD heads exposed toward the aqueous phase. Sequence-based computational tools predicted favorable physicochemical properties, with Pep1 displaying higher aqueous solubility across a range of pH conditions, while Pep2 exhibited stronger hydrophobic interactions with lipid bilayers. Experimental characterization by dynamic light scattering and zeta potential measurements indicated an increase in liposome size and a reduction in negative surface charge upon peptide incorporation. Cryogenic transmission electron microscopy revealed well-defined unilamellar structures, confirming preserved liposome morphology. Fourier-transform infrared spectroscopy further supported peptide anchoring through detectable shifts in characteristic amide and lipid peaks. Collectively, these findings indicate that Pep1 and Pep2 confer complementary advantages for liposomal surface functionalization—enhancing aqueous dispersibility and lipid affinity, respectively—offering a modular approach to engineering integrin-targeted liposomal nanocarriers.</p> Graphical abstract <p></p>

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In-silico design, characterization, and liposome anchoring simulation of amphiphilic RGD peptides for enhanced nanoparticle functionalization in integrin-targeted drug delivery

  • 期刊论文

  • 发表日期：

    2026年1月15日

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  • Adamu Safiyanu Maikifi,
  • Ismail Dwi Putra,
  • Veerakiet Boonkanokwong

摘要

Two amphiphilic peptides, Pep1 (bis(FHLAL)‑K‑RGD) and Pep2 (bis(FLIVI)‑K‑RGD), were rationally designed to achieve direct, non-covalent anchoring onto liposomal membranes for integrin-targeted drug delivery applications. The peptides were synthesized using Fmoc-based solid-phase methods and validated through high-performance liquid chromatography and mass spectrometry, confirming high purity (> 95%) and expected molecular masses. In silico analysis using coarse-grained Martini molecular dynamics simulations demonstrated successful surface anchoring of both peptides to dipalmitoyl phosphatidylcholine–cholesterol bilayers, with hydrophilic RGD heads exposed toward the aqueous phase. Sequence-based computational tools predicted favorable physicochemical properties, with Pep1 displaying higher aqueous solubility across a range of pH conditions, while Pep2 exhibited stronger hydrophobic interactions with lipid bilayers. Experimental characterization by dynamic light scattering and zeta potential measurements indicated an increase in liposome size and a reduction in negative surface charge upon peptide incorporation. Cryogenic transmission electron microscopy revealed well-defined unilamellar structures, confirming preserved liposome morphology. Fourier-transform infrared spectroscopy further supported peptide anchoring through detectable shifts in characteristic amide and lipid peaks. Collectively, these findings indicate that Pep1 and Pep2 confer complementary advantages for liposomal surface functionalization—enhancing aqueous dispersibility and lipid affinity, respectively—offering a modular approach to engineering integrin-targeted liposomal nanocarriers.

Graphical abstract