Optimized Protocol for Synthesis of Cyclic Gramicidin S:  Starting Amino Acid Is Key to High Yield

Wadhwani, Parvesh; Afonin, Sergii; Ieronimo, Marco; Buerck, Jochen; Ulrich, Anne S.

doi:10.1021/jo051519m

Cited by 62 publications

(66 citation statements)

References 77 publications

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“…The peptides were purified by HPLC with acetonitrile/water gradients, as previously described. [37][38][39] Purified peptides were characterized by analytical liquid chromatography combined with mass spectrometry (LC-MS, for details see the Supporting Information). All peptides were synthesized as C-terminal peptide amides.…”

Section: Methodsmentioning

confidence: 99%

Using the Peptide Bp100 as a Cell‐Penetrating Tool for the Chemical Engineering of Actin Filaments within Living Plant Cells

Eggenberger

Mink²,

Wadhwani³

et al. 2010

ChemBioChem

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The delivery of externally applied macromolecules or nanoparticles into living cells still represents a critically limiting step before the full capabilities of chemical engineering can be explored. Molecular transporters such as cell-penetrating peptides, peptoids, and other mimetics can be used to carry cargo across the cellular membrane, but it is still difficult to find suitable sequences that operate efficiently for any particular type of cell. Here we report that BP100 (KKLFKKILKYL-amide), originally designed as an antimicrobial peptide against plant pathogens, can be employed as a fast and efficient cell-penetrating agent to transport fluorescent test cargoes into the cytosol of walled plant cells. The uptake of BP100 proceeds slightly more slowly than the endocytosis of fluorescent dextranes, but BP100 accumulates more efficiently and to much higher levels (by an order of magnitude). The entry of BP100 can be efficiently blocked by latrunculin B; this suggests that actin filaments are essential to the uptake mechanism. To test whether this novel transporter can also be used to deliver functional cargoes, we designed a fusion construct of BP100 with the actin-binding Lifeact peptide (MGVADLIKKFESISKEE). We demonstrated that the short BP100 could transport the attached 17-residue sequence quickly and efficiently into tobacco cells. The Lifeact construct retained its functionality as it successfully labeled the actin bundles that tether the nucleus in the cell center.

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Section: Methodsmentioning

confidence: 99%

Using the Peptide Bp100 as a Cell‐Penetrating Tool for the Chemical Engineering of Actin Filaments within Living Plant Cells

Eggenberger

Mink²,

Wadhwani³

et al. 2010

ChemBioChem

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“…These values are in agreement with previous reports. [23] Some peptoid sequences proved to be inactive as antimicrobials (L5, L13, L15, C5, C13, and C15), with MIC values > 500 mg mL…”

Section: Antimicrobial and Hemolytic Activitiesmentioning

confidence: 99%

A Comparison of Linear and Cyclic Peptoid Oligomers as Potent Antimicrobial Agents

et al. 2011

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We investigated the antimicrobial activities of N-substituted glycine "peptoid" oligomers incorporating cationic and hydrophobic side chains. Head-to-tail macrocyclization was employed to enhance antimicrobial activity. Both linear and cyclic peptoids, ranging from six to ten residues, demonstrate potent antimicrobial activity against Gram-positive and Gram-negative bacteria. These peptoids do not cause significant lysis of human erythrocytes, indicating selective antimicrobial activity. Conformational ordering established upon macrocyclization is generally associated with an enhanced capacity to inhibit bacterial cell growth. Moreover, increased hydrophobic surface area also plays a role in improving antimicrobial activity. We demonstrate the potency of a cyclic peptoid in exerting antimicrobial activity against clinical strains of S. aureus while deterring the emergence of antimicrobial resistance.

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“…[42] In living systems, different internalization pathways and membrane translocation mechanisms may apply to different CPPs, depending also on the type of cargo and cell line. [23,43] Here we examine the interactions of the CPP TATA C H T U N G T R E N N U N G (48)(49)(50)(51)(52)(53)(54)(55)(56)(57)(58)(59)(60), [21,24,26,28,33,35,36,44] with phospholipid model membranes. It is an arginine-rich sequence consisting of 13 amino acids (GRKKRRQRRRPPQ), derived from the basic domain of the HIV-1 protein Tat (to distinguish the parent protein "Tat" from the derived peptide "TAT" we use these different forms of capitalization throughout the text).…”

Section: Introductionmentioning

confidence: 99%

The Cell‐Penetrating Peptide TAT(48‐60) Induces a Non‐Lamellar Phase in DMPC Membranes

et al. 2006

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Cell-penetrating peptides (CPPs) are short polycationic sequences that can translocate into cells without disintegrating the plasma membrane. CPPs are useful tools for delivering cargo, but their molecular mechanism of crossing the lipid bilayer remains unclear. Here we study the interaction of the HIV-derived CPP TAT (48-60) with model membranes by solid-state NMR spectroscopy and electron microscopy. The peptide induces a pronounced isotropic (31)P NMR signal in zwitterionic DMPC, but not in anionic DMPG bilayers. Octaarginine and to a lesser extent octalysine have the same effect, in contrast to other cationic amphiphilic membrane-active peptides. The observed non-lamellar lipid morphology is attributed to specific interactions of polycationic peptides with phosphocholine head groups, rather than to electrostatic interactions. Freeze-fracture electron microscopy indicates that TAT(48-60) induces the formation of rodlike, presumably inverted micelles in DMPC, which may represent intermediates during the translocation across eukaryotic membranes.

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Optimized Protocol for Synthesis of Cyclic Gramicidin S: Starting Amino Acid Is Key to High Yield

Cited by 62 publications

References 77 publications

Using the Peptide Bp100 as a Cell‐Penetrating Tool for the Chemical Engineering of Actin Filaments within Living Plant Cells

Using the Peptide Bp100 as a Cell‐Penetrating Tool for the Chemical Engineering of Actin Filaments within Living Plant Cells

A Comparison of Linear and Cyclic Peptoid Oligomers as Potent Antimicrobial Agents

The Cell‐Penetrating Peptide TAT(48‐60) Induces a Non‐Lamellar Phase in DMPC Membranes

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