Study of the nano-morphological versatility by self-assembly of a peptide mimetic molecule in response to physical and chemical stimuli

Kar, Sudeshna; Wu, Kung-Wei; Hsu, I‐Jui; Lee, Chi-Rung; Tai, Yian

doi:10.1039/c3cc49769k

Cited by 11 publications

(22 citation statements)

References 24 publications

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“…30 In the case of peptide 2, IR results also remain similar in the as-synthesized form and in the nano-tube form ( Table S5 in the ESI †). Thus, in a peptide sequence simple reversal of position of two rigid amino acids can cause marked difference in self-assembled structure and nano-morphologies, which may nd its application in the model study of different peptide interaction behaviors for isomeric peptides in a biological system and in explaining the structural correlation with morphological difference of isomeric peptides/proteins.…”

Section: Resultssupporting

confidence: 58%

“…1 and ref. 30). The number density and the diameter of the spheres generated by peptide 1 and tubes generated by peptide 2 vary with respect to the peptide concentrations in methanolic solution (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Detailed synthesis of Boc-m-ABA-Aib-OMe (peptide 1) and Boc-Aib-m-ABA-OMe (peptide 2) has been described in ref. 30 and ESI †, respectively. The reported compounds were fully characterised by IR, NMR and mass spectroscopy and by X-ray crystallography.…”

Section: Methodsmentioning

confidence: 99%

“…1,2 Reversal of sequence is one of the most common types of positional isomerism among peptides which has been recognized to affect bio-activities signicantly. For example, it has been observed that reversal of sequence in bamyloid peptide (Ab), aggregation of which causes Alzheimer's disease, brings changes in neurotoxicity of Ab; such as, the reverse analogue of extremely neurotoxic fragment Ab (25)(26)(27)(28)(29)(30)(31)(32)(33)(34)(35)) of b-amyloid peptide, Ab(35-25), has been found to be nonneurotoxic. 3 Again two antimicrobial peptides, cecropin P (CP1) and its retro analogue, have shown marked difference in biological activity conrming the fact that peptide sequence is the determining factor for their bio-activity.…”

Section: Introductionmentioning

confidence: 99%

“…4 Moreover, it has been found that reversal of the positions of amino acid residues also affects stability towards the secondary structure of peptides. 5 Interestingly, the most important fragment of b-amyloid peptide that correlates with Alzheimer's disease, Ab (25)(26)(27)(28)(29)(30)(31)(32)(33)(34)(35), forms small plate-like "shards" having well-dened edges but no such detectable morphology is observed in the case of its retro analogue Ab ; rather an amorphous material is found. 6 Therefore positional isomerism affects the morphology of peptides to a great extent, which may create immense change in their biological activity.…”

Section: Introductionmentioning

confidence: 99%

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Marked difference in self-assembly, morphology, and cell viability of positional isomeric dipeptides generated by reversal of sequence

Kar

Tai

2015

Soft Matter

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In this study two positional isomeric dipeptides Boc-m-ABA-Aib-OMe () and Boc-Aib-m-ABA-OMe () synthesized by reversal of the positions of two rigid amino acids (m-ABA: m-aminobenzoic acid, Aib: α-aminoisobutyric acid) showed marked difference in morphology under the same environmental conditions. Investigation of single crystal structures reveals the difference in crystal packing and higher order self-assembly pattern for both the isomeric peptides, which might be the responsible factor for their different morphological patterns. Moreover, these isomeric dipeptides have produced different cellular viability effects towards normal bone cells. These two peptides would have utilities in the model study of isomeric peptides/proteins, where morphological difference under identical conditions brings changes in their individual bio-activities and where the reversal of sequence causes different cellular viability and generates health hazard.

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Section: Resultssupporting

confidence: 58%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Marked difference in self-assembly, morphology, and cell viability of positional isomeric dipeptides generated by reversal of sequence

Kar

Tai

2015

Soft Matter

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Engineering Ionophore Gramicidin‐Inspired Self‐Assembled Peptides for Drug Delivery and Cancer Nanotherapeutics

Chakraborty

Dutta

Mukherjee

et al. 2018

Advanced Therapeutics

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Nature‐inspired self‐assembled peptide‐based nanoscale materials are of great interest for biomedical applications. Here, ionophore gramicidin‐inspired designed nanoscale materials for drug delivery and cancer nanotherapeutics are reported. The length dependent formation of diverse nanoarchitectures by experimental and computational studies from gramicidin‐inspired sequences is explored and their therapeutic potential is evaluated. Mechanistic studies revealed that gramicidin A (gA) and gramicidin‐inspired octapeptide (LD8) induce cytotoxic effects, mitochondrial depolarization, and apoptotic cell death against metastatic breast cancer cell line MDA‐MB‐231. Doxorubicin loaded LD8 peptide (LD8‐Dox‐NP) and doxorubicin loaded gramicidin (gA‐Dox‐NP) show cytotoxicity determined by MTT assay and apoptosis as evidenced by DNA fragmentation study and Western blot analysis of poly (ADP‐ribose) polymerase (PARP) expression and cleavage. gA‐Dox‐NP and LD8‐Dox‐NP treated MDA‐MB‐231 cells show upregulation of tumor suppressor protein p53, which can inhibit cell proliferation. Interestingly, cell cycle analysis suggests that gA‐Dox‐NP and LD8‐Dox‐NP induce S and G2 phase cell cycle arrest, respectively. These data establish gA and LD8 peptide as new potential anticancer therapeutics against metastatic breast cancer and suggest that gA‐Dox‐NP and LD8‐Dox‐NP can be potentially used as two‐in‐one nanomedicine for treating breast cancer.

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Vesicles mimicking normal and cancer cell membranes exhibit differential responses to the cell-penetrating peptide Pep-1

Almarwani

Phambu

Alexander

et al. 2018

Biochimica et Biophysica Acta (BBA) - Biomembranes

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The cell-penetrating peptide (CPP) Pep-1 presents a great potential in drug delivery due to its intrinsic property to cross plasma membrane. However, its mechanism of entry into the cell remains unresolved. In this study, we compare the selectivity of Pep-1 towards vesicles mimicking normal and cancer cell membranes. The interaction was performed in a wide range of peptide-to-lipid molar ratios using infrared (IR), fluorescence, scanning electron microscopy (SEM), thermogravimetric analysis (TGA) and differential scanning calorimetry (DSC) techniques. At low peptide concentration, fluorescence experiments show that lipid-phosphatidylserine (PS) seems to enable Pep-1 translocation into cancer cell membrane as evidenced by the blue shift of its maximal emission wavelength. DSC data show that Pep-1 induces segregation of lipids. At high peptide concentration, IR data indicate that the interaction of Pep-1 is relatively stronger with normal cell membrane than with cancer cell membrane through the phosphate groups, while the interaction is weaker with normal cell membrane than with cancer cell membrane through the carbonyl groups. TGA and DSC data reveal that vesicles of normal cell membrane are thermally more stable than vesicles of cancer cell membrane. This suggests that the additional lipid PS included in cancer cell membrane has a destabilizing effect on the membrane structure. SEM images reveal that Pep-1 form superstructures including spherical particles and fibrils in the presence of both model membranes. PS seems to enhance peptide transport across cellular membranes. The biophysical techniques in this study provide valuable insights into the properties of CPPs in drug delivery systems.

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Study of the nano-morphological versatility by self-assembly of a peptide mimetic molecule in response to physical and chemical stimuli

Abstract: A small peptide mimetic molecule can form diverse nanostructures such as nano-vesicles, nano-tubes and nano-ribbons/fibrils by self-assembly, in response to various physical and chemical stimulations.

Cited by 11 publications

References 24 publications

Marked difference in self-assembly, morphology, and cell viability of positional isomeric dipeptides generated by reversal of sequence

Marked difference in self-assembly, morphology, and cell viability of positional isomeric dipeptides generated by reversal of sequence

Engineering Ionophore Gramicidin‐Inspired Self‐Assembled Peptides for Drug Delivery and Cancer Nanotherapeutics

Vesicles mimicking normal and cancer cell membranes exhibit differential responses to the cell-penetrating peptide Pep-1

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