Structural-features of food-derived bioactive peptides with anti-inflammatory activity: A brief review

Abstract

Chronic inflammatory conditions such as obesity, type-2 diabetes, and cardiovascular diseases are the leading causes of mortality worldwide. Hence, much research interest in bioactive peptides has been stimulated due to lack of potent pharmacological interventions. Although many such peptides have been identified from food proteins, insufficient information is available on their structurefunction relationship. Presence of hydrophobic and positively charged amino acids is a common occurrence for the peptides with anti-inflammatory properties. However, inconsistent findings have also been reported. Most of the food-derived peptides exhibited their anti-inflammatory activities primarily by inhibiting signaling components of either NF-jB or MAPK pathway, which are the two major pathways involved in chronic inflammation following uncontrolled signal activation. This review highlighted the structural requirements of the peptides to exhibit antiinflammatory activity based on the current knowledge about food-derived anti-inflammatory peptides and their underlying molecular mechanisms of action. Practical applicationsWhile research in the food-derived bioactive peptide is gaining momentum, but the ability to translate these new findings into the commercial product such as nutraceuticals and functional foods, remains delayed. The most prominent reasons for this delay are the lack of detailed research on, (i) the structure-function relationship of the peptide and the underlying molecular mechanisms of these bioactive peptides, and (ii) the interaction of these peptides with different cellular elements in the disease pathophysiology. This review gives an insight into the structure-activity relationship of bioactive peptides involved in anti-inflammatory responses. The information provided here would be highly beneficial to describe the possible anti-inflammatory activity of any newly identified peptides from different food sources. K E Y W O R D Santi-inflammation, bioactive peptides, food proteins, inflammatory responses, structure-function relationships

Diet, Lifestyle and Cardiovascular Diseases: Linking Pathophysiology to Cardioprotective Effects of Natural Bioactive Compounds

“…CV diseases are the leading cause of death globally [129]. The importance of diet in the increasing prevalence of CV risk factors, including serum lipid levels, glucose levels, hypertension, obesity, endothelial dysfunction, inflammation and/or oxidative stress been well established in the literature [130][131][132] (Table 2).…”

Bioactive peptides from food fermentation: A comprehensive review of their sources, bioactivities, applications, and future development

“…In support, Guha & Majumder (2019) also reported that the peptides that are responsible for anti‐inflammatory activity contain at least one residue of glutamine such as IQW, QEPV, QCQQAVQSAV, QCQQCAVGEGGL, and lunasin (SKWQHQQDSCRKQLQGVNLTPCEKHIMQKIQGRGDDDDDDDDD). It was reported that regardless of length, anti‐inflammatory peptides are rich in hydrophobic amino acids and these amino acids are primarily grouped toward the N‐terminus, whereas at the C‐terminal region contains mostly polar amino acids (Guha & Majumder, 2019). Nan et al.…”

“…González-Montoya et al (2018) suggested that peptides with glutamine residue may exert anti-inflammatory activity as they found that the peptides of 5 to 10 kDa from germinated soybean protein after simulated gastrointestinal digestion contained at least one glutamine residue in the most active fraction. In support, Guha & Majumder (2019) also reported that the peptides that are responsible for anti-inflammatory activity contain at least one residue of glutamine such as IQW, QEPV, QCQQAVQSAV, QCQQCAVGEGGL, and lunasin (SKWQHQQDSCRKQLQGVNLTPCEKHIMQK-IQGRGDDDDDDDDD). It was reported that regardless of length, anti-inflammatory peptides are rich in hydrophobic amino acids and these amino acids are primarily grouped toward the N-terminus, whereas at the Cterminal region contains mostly polar amino acids (Guha & Majumder, 2019).…”

“…In support, Guha & Majumder (2019) also reported that the peptides that are responsible for anti-inflammatory activity contain at least one residue of glutamine such as IQW, QEPV, QCQQAVQSAV, QCQQCAVGEGGL, and lunasin (SKWQHQQDSCRKQLQGVNLTPCEKHIMQK-IQGRGDDDDDDDDD). It was reported that regardless of length, anti-inflammatory peptides are rich in hydrophobic amino acids and these amino acids are primarily grouped toward the N-terminus, whereas at the Cterminal region contains mostly polar amino acids (Guha & Majumder, 2019). Nan et al (2009) found that highly hydrophobic peptides promote peptide binding to membranes and membrane depolarization in microbial cells, indicating that highly hydrophobic amino acids enhance the peptide-cell membrane interaction, which, in turn, modulate the downstream signaling pathways and subsequently exerting anti-inflammatory effect.…”

“…The positively charged amino acids like arginine and lysine do not have a fixed position in the anti‐inflammatory peptides. They can be found either at the C‐terminus, N‐terminus, or in the middle of the sequence (Guha & Majumder, 2019). Although peptides with positively charged amino acids have shown anti‐inflammatory property, peptides such as pEL, γ‐EC, and γ‐EV that contain negatively charged glutamate amino acid also exhibit excellent anti‐inflammatory activity (Hirai et al., 2014; Zhang et al., 2015).…”