Prostatic Acid Phosphatase (248-286), PAP (248-286)

Product Name: Prostatic Acid Phosphatase (248-286), PAP (248-286)

Sequence One Letter Code: GIHKQKEKSRLQGGVLVNEILNHMKRATQIPSYKKLIMY

Sequence Three Letter Code: H-Gly-Ile-His-Lys-Gln-Lys-Glu-Lys-Ser-Arg-Leu-Gln-Gly-Gly-Val-Leu-Val-Asn-Glu-Ile-Leu-Asn-His-Met-Lys-Arg-Ala-Thr-Gln-Ile-Pro-Ser-Tyr-Lys-Lys-Leu-Ile-Met-Tyr-OH

Chemical Formula:C203H342N60O54S2

Molecular Weight: 4551.7

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: Antiviral

Source / Species: Human, gorilla

Conjugation: Unconjugated

Code Nacres: NA.26

Application: This peptide corresponds to residues 248–286 of human prostatic acid phosphatase and forms the core component of semen-derived enhancer of viral infection (SEVI). The peptide can self-assemble into amyloid fibrils that strongly enhance HIV infection by promoting virion attachment and fusion with target cells. SEVI fibrils are thought to facilitate viral transmission by neutralizing electrostatic repulsion between viral particles and host cell membranes. Because of this property, the peptide is widely used in virology research investigating host factors that influence viral infectivity and mucosal transmission. It supports studies examining amyloid-virus interactions, mechanisms of HIV entry, and strategies aimed at inhibiting sexually transmitted viral infections. The peptide is also useful for exploring the biological roles of functional amyloids.

Current Research: Introduction to SEVI and Viral Transmission The PAP248–286 peptide is derived from residues 248–286 of human prostatic acid phosphatase (PAP) and represents the core component of semen-derived enhancer of viral infection (SEVI). This peptide has gained considerable attention in virology because of its ability to self-assemble into amyloid fibrils that significantly enhance the infectivity of certain viruses, particularly HIV. Unlike pathological amyloids associated with neurodegenerative diseases, SEVI represents a functional amyloid formed under physiological conditions. Its interaction with viral particles and host cells provides an important experimental model for studying how host-derived factors influence viral transmission and infection efficiency. Structural Characteristics of PAP248–286 The PAP248–286 peptide contains a sequence that promotes self-assembly into β-sheet–rich amyloid fibrils. Under appropriate conditions, the peptide aggregates to form stable fibrillar structures characteristic of amyloid assemblies. These fibrils exhibit a positively charged surface, which is a key feature responsible for their biological activity. Viral particles and host cell membranes typically carry negative surface charges. The SEVI fibrils help overcome electrostatic repulsion between these surfaces, enabling closer contact between virions and target cells. Because the peptide reliably forms amyloid fibrils in vitro, it is widely used in structural and biochemical experiments investigating amyloid formation and function. Mechanism of Viral Infection Enhancement SEVI fibrils derived from the PAP248–286 peptide enhance viral infection by facilitating the interaction between viral particles and host cells. The fibrils act as molecular bridges that capture virions and promote their attachment to cell membranes. This process increases the local concentration of virus particles near target cells and promotes membrane fusion events required for viral entry. In the context of HIV infection, SEVI has been shown to dramatically increase the efficiency with which the virus infects susceptible cells. The ability of SEVI to neutralize electrostatic barriers between viral particles and host cells is considered a major factor contributing to this enhancement of viral infectivity. Applications in HIV and Virology Research Because of its role in promoting viral entry, the PAP248–286 peptide is widely used in HIV research and studies of sexually transmitted viral infections. Researchers use the peptide to investigate how host-derived factors influence viral transmission and infection dynamics. In experimental systems, SEVI fibrils provide a useful model for studying virus–host interactions during the early stages of infection. By examining how the peptide interacts with viral particles and cellular membranes, scientists can gain insight into mechanisms that facilitate viral attachment and entry. These studies contribute to a broader understanding of viral transmission pathways, particularly in mucosal environments. Investigating Amyloid–Virus Interactions The PAP248–286 peptide is also valuable for studying interactions between amyloid structures and viral particles. Unlike disease-associated amyloids, SEVI represents an example of a naturally occurring amyloid that performs a functional biological role. Researchers use this peptide to explore how amyloid fibrils interact with biological membranes and pathogens. Such investigations provide insight into the structural properties of amyloids and how they influence biological processes beyond neurodegenerative disease. These experiments also help clarify how amyloid structures can act as scaffolds that facilitate molecular interactions in complex biological systems. Applications in Antiviral Strategy Development Because SEVI fibrils can significantly enhance viral infection, they have become a target of interest in studies aimed at developing strategies to inhibit viral transmission. Researchers use the PAP248–286 peptide to test compounds or interventions that disrupt amyloid formation or block fibril–virus interactions. Compounds capable of preventing SEVI fibril formation or interfering with fibril–virion binding may reduce viral infectivity in experimental models. These approaches contribute to research exploring preventive strategies against sexually transmitted viral infections. Functional Amyloids and Biological Significance The PAP248–286 peptide has also contributed to growing interest in functional amyloids, a class of amyloid structures that perform beneficial biological roles rather than causing disease. Functional amyloids are increasingly recognized in diverse biological systems, where they can participate in processes such as structural organization, signaling, and host defense. Studying SEVI provides an opportunity to understand how amyloid structures form, interact with biological molecules, and influence cellular processes. Conclusion The PAP248–286 peptide, derived from human prostatic acid phosphatase, forms the core component of semen-derived enhancer of viral infection (SEVI). Through self-assembly into amyloid fibrils, the peptide enhances viral infectivity by promoting the interaction between virions and host cell membranes. Widely used in virology, HIV research, and studies of amyloid biology, this peptide supports investigations into virus–host interactions, mechanisms of viral entry, and strategies for inhibiting viral transmission. Its role as a functional amyloid also provides valuable insight into the broader biological functions of amyloid structures.