Peptide based therapeutics and their use for the treatment of neurodegenerative and other diseases

Baig, Mohammad Hassan; Ahmad, Khurshid; Saeed, Mοhd; Alharbi, Ahmed; Barreto, George E.; Ashraf, Ghulam Md; Choi, Inho

doi:10.1016/j.biopha.2018.04.025

Cited by 90 publications

(65 citation statements)

References 129 publications

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“…However, numerous computational techniques have evidenced the structural and functional insights into the architecture of protein-peptide interfaces for the rational peptide design approach. These methods help to fulfill the vision of computationally designed peptides for therapies through the high-resolution structures of protein-peptide complexes [64][65][66]. In vivo studies have found that anti-hypertensive effects can be attained in humans through peptides especially di-and/or tri-peptides [67NR,68].…”

Section: Derived Peptidesmentioning

confidence: 99%

In Silico identification of angiotensin-converting enzyme inhibitory peptides from MRJP1

Tahir¹,

Bashir²,

Yousaf³

et al. 2020

PLoS ONE

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Hypertension is considered as one of the most common diseases that affect human beings (both male and female) due to its high prevalence and also extending widely to both industrialize and developing countries. Angiotensin-converting enzyme (ACE) has a significant role in the regulation of blood pressure and ACE inhibition with inhibitory peptides is considered as a major target to prevent hypertension. In the current study, a blood pressure regulating honey protein (MRJP1) was examined to identify the ACE inhibitory peptides. The 3D structure of MRJP1 was predicted by utilizing the threading approach and further optimized by performing molecular dynamics simulation for 30 nanoseconds (ns) to improve the quality factor up to 92.43%. Root mean square deviation and root mean square fluctuations were calculated to evaluate the structural features and observed the fluctuations in the timescale of 30 ns. AHTpin server based on scoring vector machine of regression models, proteolysis and structural characterization approaches were implemented to identify the potential inhibitory peptides. The anti-hypertensive peptides were scrutinized based on the QSAR models of anti-hypertensive activity and the molecular docking analyses were performed to explore the binding affinities and potential interacting residues. The peptide "EALPHVPIFDR" showed the strong binding affinity and higher anti-hypertensive activity along with the global energy of-58.29 and docking score of 9590. The aromatic amino acids especially Tyr was observed as the key residue to design the dietary peptides and drugs like ACE inhibitors.

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Section: Derived Peptidesmentioning

confidence: 99%

In Silico identification of angiotensin-converting enzyme inhibitory peptides from MRJP1

Tahir¹,

Bashir²,

Yousaf³

et al. 2020

PLoS ONE

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“…Our group has also been focusing on combining the inhibitory properties of inhibitor peptides with CPPs [ 381 ]. Peptide vaccines (reviewed by Baig et al [ 382 ]) have also gained interest in the immunotherapy of different types of cancer [ 383 ] such as breast cancer [ 384 , 385 ] or lung cancer [ 386 ], virally mediated diseases such as influenza [ 387 ], Human papilloma virus (HPV) [ 388 , 389 ], and HIV, and neurodegenerative diseases [ 382 ] such as Alzheimer’s [ 390 ]. These peptide vaccines are frequently delivered as emulsions [ 391 ] to facilitate uptake across the membrane.…”

Section: Future Perspectives: Characterizing Membrane Active Peptmentioning

confidence: 99%

Membrane Active Peptides and Their Biophysical Characterization

2018

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In the last 20 years, an increasing number of studies have been reported on membrane active peptides. These peptides exert their biological activity by interacting with the cell membrane, either to disrupt it and lead to cell lysis or to translocate through it to deliver cargos into the cell and reach their target. Membrane active peptides are attractive alternatives to currently used pharmaceuticals and the number of antimicrobial peptides (AMPs) and peptides designed for drug and gene delivery in the drug pipeline is increasing. Here, we focus on two most prominent classes of membrane active peptides; AMPs and cell-penetrating peptides (CPPs). Antimicrobial peptides are a group of membrane active peptides that disrupt the membrane integrity or inhibit the cellular functions of bacteria, virus, and fungi. Cell penetrating peptides are another group of membrane active peptides that mainly function as cargo-carriers even though they may also show antimicrobial activity. Biophysical techniques shed light on peptide–membrane interactions at higher resolution due to the advances in optics, image processing, and computational resources. Structural investigation of membrane active peptides in the presence of the membrane provides important clues on the effect of the membrane environment on peptide conformations. Live imaging techniques allow examination of peptide action at a single cell or single molecule level. In addition to these experimental biophysical techniques, molecular dynamics simulations provide clues on the peptide–lipid interactions and dynamics of the cell entry process at atomic detail. In this review, we summarize the recent advances in experimental and computational investigation of membrane active peptides with particular emphasis on two amphipathic membrane active peptides, the AMP melittin and the CPP pVEC.

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“…The 200-µL samples were transferred to a black 96-well microplate, and the fluorescence was measured for 10 min (excitation: 350 nm; emission: 420 nm) [14]. The depolarization of the bacterial cytoplasmic membrane by the peptide was evaluated using 3, 3 -dipropylthiadicarbocyanine iodide (DiSC 3 (5), Sigma-Aldrich). The bacteria were diluted to 1 × 10 7 CFU/mL in HEPES buffer.…”

Section: Membrane Permeability Testmentioning

confidence: 99%

“…Owing to their chemical and physiological nature, the utilization and optimization of peptides can facilitate rapid drug designing. Moreover, combined treatment using conventional medication with peptides has reportedly demonstrated synergistic effects on pathological phenomena such as infectiona, cancera, and neurodegeneration [3][4][5]. As the biological value of peptides increases, the identification of novel peptides and investigation of their functionalities are gaining more interest.…”

Section: Introductionmentioning

confidence: 99%

Antibacterial and Anti-Inflammatory Effects of Novel Peptide Toxin from the Spider Pardosa astrigera

Shin¹,

Hwang²,

Kim³

et al. 2020

Antibiotics

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The prevalence of antibiotic-resistant bacteria has become an immediate threat to public health. Antimicrobial peptides are attracting attention as a new source of antibiotics due to their ability to prevent drug-resistances with fewer side effects. Spider venom is composed of various bioactive substances with multiple functionalities such as antimicrobial and anti-inflammatory effects. Here, RNA sequencing was conducted on the venom gland of the spider Pardosa astrigera, and a potential toxin peptide with antibacterial properties was selected via homology and in silico analysis. A novel toxin, Lycotoxin-Pa4a, inhibited both gram-negative and gram-positive bacteria by disrupting the outer and bacterial cytoplasmic membrane. Moreover, the peptide downregulated the expression of pro-inflammatory mediators while upregulating the level of anti-inflammatory cytokine by inactivating mitogen-activated protein kinase signaling in a lipopolysaccharide-stimulated murine macrophage cell line. In this research, we identified a novel peptide toxin, Lycotoxin-pa4a, with antibacterial and anti-inflammatory properties, suggesting its potential for the development of a new antibiotics, as well as offering insights into the utilization of biological resources.

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Peptide based therapeutics and their use for the treatment of neurodegenerative and other diseases

Cited by 90 publications

References 129 publications

In Silico identification of angiotensin-converting enzyme inhibitory peptides from MRJP1

In Silico identification of angiotensin-converting enzyme inhibitory peptides from MRJP1

Membrane Active Peptides and Their Biophysical Characterization

Antibacterial and Anti-Inflammatory Effects of Novel Peptide Toxin from the Spider Pardosa astrigera

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