Abstract: Fatty acid binding proteins(FABPs) are a family of small molecular weight proteins derived from a common ancestral gene. They are widely distributed in various tissues including the intestines, heart, brain, adipose tissue and muscles. FABPs exhibit specific binding capabilities for fatty acids and are responsible for transporting these fatty acids to organelles such as peroxisomes, mitochondria and the cell nucleus, thereby regulating processes related to fatty acid oxidation, triglyceride, and phospholipid synthesis within cellular metabolism. This review article explored the classification, structural characteristics, biological functions, and research progress on typical invertebrates(protozoa, arthropods, mollusks and echinoderms) FABPs. It was found that invertebrate FABPs lacked functional groups such as sugars, water molecules, amino and thiol groups in their molecular structure, suggesting a more complex functionality related to growth, development and fatty acid transport. In comparison to vertebrates, research on invertebrate FABPs was still in its nascent stage, further investigation should focus on their gene structure, protein construction, biological functions, including elucidating their role as intracellular carriers of fatty acids to identify specific membrane ligand recognition sites in invertebrates, confirming whether FABPs molecular structures possessed the capability to capture or release ligands, analyzing the relationship between ligand binding specificity and the physicochemical properties of β-barrel folddefined cavity surface coatings, and exploring potential differences in features and biological functions across different types of FABPs. Additionally, certain FABPs isolated from invertebrates have shown promising applications in the preparation of biogenic vaccines, thus potentially contributing to aquaculture breeding and the prevention and treatment of metabolic diseases, providing new perspectives for the prevention and treatment of metabolic diseases in intensive aquaculture models.